The polyclonal antibody recognizes human intestinal fatty acid binding protein (I-FABP) of both natural and recombinant origin. The I-FABP protein is derived from the human FABP2 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. I-FABP is localized in the small bowel epithelium, with highest expression level in the jejunum.
The monoclonal antibody K5A6 recognizes human liver fatty acid binding protein (L-FABP) of both natural and recombinant origin. The L-FABP protein is derived from the human FABP1 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. L-FABP is localized in the liver, kidney and intestinal epithelium. The monoclonal antibody K5A6 is useful to detect ischemic areas of human liver.
The monoclonal antibody L2B10 recognizes human liver fatty acid binding protein (L-FABP) of both natural and recombinant origin. The L-FABP protein is derived from the human FABP1 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. L-FABP is localized in the liver, kidney and intestinal epithelium. The monoclonal antibody L2B10 is useful to detect ischemic areas of human liver. Furthermore, the antibody can be used for the purification of human L-FABP.
Antibody Isotype:
IgG2b
Monosan Range:
MONOSAN
Clone:
L2B10
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Bax; D et al. Scand J Gastroenterology 2007; 42: 902
The monoclonal antibody 67D3 recognizes human heart-type fatty acid-binding protein (H-FABP) of both natural and recombinant origin. The H-FABP protein is derived from the human FABP3 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. H-FABP is localized in the heart, skeletal and smooth muscle, mammary epithelial cells, aorta, distal tubules of the kidney, lung, brain, placenta, and ovary. Furthermore, this antibody is useful for the purification of H-FABP.
The monoclonal antibody 66E2 recognizes human heart fatty acid binding protein (H-FABP) of both natural and recombinant origing. The H-FABP protein is derived from the human FABP3 gene. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity that bind long chain fatty acids. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas. H-FABP is localized in the heart, skeletal and smooth muscle, mammary epithelial cells, aorta, distal tubules of the kidney, lung, brain, placenta, and ovary. The monoclonal antibody 66E2 stains heart muscle cells and striated skeletal muscle cells in immunohistology. It can be used to detect ischemia areas of human heart. It is also useful as marker for brain damage. Furthermore, this antibody is useful for the purification of H-FABP.
Antibody Isotype:
IgG1
Monosan Range:
MONOSAN
Clone:
66E2
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Roos; W et al. J Immunol Meth 1995; 183: 149
References 2:
Guillaume, E et al Proteomics 2003, 3: 1495
References 3:
Zimmermann-Ivol; C et al. Mol Cell Proteomics 2004; 3: 66
Rabbit anti-Beta Amyloid Polyclonal Antibody (Unconjugated), suitable for ELISA.
Background Info:
The beta Amyloid peptide is derived from the cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. Beta amyloid peptides are the major constituents of the plaques and tangles that occur in Alzheimer's disease.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Host Animal:
Rabbit
Species Reactivity:
Human
Immunogen:
A synthetic peptide (DAEFRHDSGYEVHH) conjugated to bovine serum albumin (BSA) corresponding to amino acid sequence 1-14 of mature human beta amyloid.
Applications:
ELISA
Antibody Isotype:
Mixed
Application Details:
ELISA. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.
Human beta amyloid, cross reactivity to APP has not bee tested.
Storage:
At least 12 months after purchase at 2-8°C (lyophilized formulations). After reconstitution, aliquot and store at -20°C for a higher stability and at 2-8°C with an appropriate antibacterial agent. Avoid freeze-thaw cycles.
The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (A? associated with the pathology characteristic of Alzheimer's disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal A? accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for A? have been shown to actually detect intraneuronal APP and not A? exclusively.<br /><br />MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide. <strong>MOAB-2 did not detect APP or APP-CTFs</strong> in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice). <br /><br />Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for A?40 and A?42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10. In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal A?, distinct from A? associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.<br /><br />Biosensis now offers <strong>biotinylated MOAB-2</strong> <strong>antibody</strong> allowing more flexibility in experimental design by using the biotin-avidin/streptavidin detection method. Biotinylated MOAB-2 antibody may also help to reduce background staining in difficult-to-stain tissues and increase detection sensitivity. The ability of biotinylated MOAB-2 antibody to detect amyloid beta has been validated by IHC.<br /><br />Purified, non-biotinylated MOAB-2 antibody is available <a href="https://www.biosensis.com/moab-mouse-monoclonal-antibody-amyloid-beta-peptide-beta-4042-purified-p-1181.htmL">here</a>.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized from PBS buffer, pH 7.4; contains no preservative.
Host Animal:
Mouse
Species Reactivity:
Human,Rat
Immunogen:
Recombinant human amyloid beta protein 42 (A?42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Applications:
ELISA,ICC,IHC-Frozen,IHC-Paraffin-embedded,IP,WB
Clone number:
MOAB-2
Antibody Isotype:
IgG2b, lambda
Application Details:
The biotinylated MOAB-2 antibody has been tested by IHC (1:500 - 1:2,000 dilution) and is also expected to work in applications validated for the unlabelled antibody (M-1586-100) at same or higher dilutions: Western Blotting (WB), Immunohistochemistry (IHC), Immunohistochemistry/paraffin embedded IHC(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA.<br><br><i>Western Blotting:</i><br><br>MOAB-2 has been tested in WB using purified synthetic beta-amyloid preparations and from transgenic mouse brain formic acid extracts (see Figure 1). Formic acid extraction/concentration is required for western blot detection from extracts. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. <br><br>Tissue samples for the detection of beta-amyloid should be prepared as detailed in Youmans KL et al., 2011 (Journal of Neuroscience Methods 196: 51-59) for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans KL et al., 2012. <br><br><i>Immunohistochemistry:</i><br><br>Suggested dilution for biotinylated MOAB-2 in IHC is 1:500-1:2,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Antigen retrieval is required in fixed tissues for optimal staining.<br><br>Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP (Youmans KL et al., 2012).<br><br>The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER). Recommended buffer for HIER is citrate, pH 6.0. Signal was weak without antigen retrieval. Immunoreactivity was observed in intraneural-amyloid deposition (plaque) in Alzheimer's brain. MOAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining.<br><br>In addition, MOAB-2 demonstrated no significant differences in A-beta detection using paraffin fixed, free-floating sections (Youmans KL et al., 2012). Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular A-beta compared to without FA (incubated in 88% FA 8 min, Youmans KL et al., 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 x 10 min), blocked with 3% horse serum in TBSX (3 x 10 min) followed by 1% horse serum in TBSX (2 x10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al., 2012, for full IHC(P) protocol and method details.<br><br><i>Immunofluorescence:</i><br><br>For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 x 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 x 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies (Youmans KL et al., 2012).<br><br><i>Immunoprecipitation:</i><br><br>For IP, the suggested dilution is 1:200 to 1:1,000 for labelled beta-amyloid using SA-coated beads as the capture vehicle, similar to the protocols employed by Youmans KL et al., 2012.<br><br><i>ELISA:</i><br><br>In an ELISA, a dilution of 1:50-1:1,000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. <br><br>Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.
Kim, S. et al. (2020) Performance Validation of a Planar Hall Resistance Biosensor through Beta-Amyloid Biomarker. Sensors (Basel). 20(2) Application: In-vitro biosensor. Ruan, CS. et al. (2017) Sortilin inhibits amyloid pathology by regulating non-specific degradation of APP. Exp Neurol. [Epub ahead of print] Application: IHC References for non-biotinylated MOAB-2 antibody (M-1586-100): Zhu, B. et al. (2017) ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating _-secretase activity. Nat Commun. 8(1):1472. Application: IHC Huang, TY. et al. (2017) SORLA attenuates EphA4 signaling and amyloid _-induced neurodegeneration. J Exp Med. pii: jem.20171413. [Epub ahead of print]. Application: IHC Felecia, M. et al. (2017) Peripheral Inflammation, Apolipoprotein E4, and Amyloid-_ Interact to Induce Cognitive and Cerebrovascular Dysfunction. ASN Neuro. 9(4):1759091417719201. Application: IHC/IF Thomas, R. et al. (2016) Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice. Acta Neuropathol Commun. 4(1):111 Application: IHC Koster, KP. et al. (2016) Epidermal growth factor prevents oligomeric amyloid-_ induced angiogenesis deficits in vitro. J Cereb Blood Flow Metab. [Epub ahead of print] Application: IF Loffler, T. et al. (2016) Decreased Plasma A? in Hyperlipidemic APPSL Transgenic Mice Is Associated with BBB Dysfunction. Front. Neurosci. Application: IF Kobro-Flatmoen, A. et al. (2016) Reelin-immunoreactive neurons in entorhinal cortex layer II selectively express intracellular amyloid in early Alzheimer's disease. Neurobiology of Disease. 93:172-183. Application: IHC Tai, LM. et al. (2016) The role of APOE in cerebrovascular dysfunction. Acta Neuropathol. 131(5):709-23. Application: IF Kim, YH. et al. (2015) A 3D human neural cell culture system for modeling Alzheimer's disease. Nat Prot. 10(7):985-1006. Application: WB Condello, C. et al. (2015) Microglia constitute a barrier that prevents neurotoxic protofibrillar A?42 hotspots around plaques. Nat Commun. 6:6176. Application: IF Iulita MF et al (2014) Intracellular Abeta pathology and early cognitive impairments in a transgenic rat model overexpressing human amyloid precursor protein: a multidimensional study. Acta Neuropathol Commun. 6:61. Application: IF, IH Smith BR et al (2014) Neuronal inclusions of alpha-synuclein contribute to the pathogenesis of Krabbe disease. J Pathol. Apr;235(5):509-21. Application: IF
Specificity:
MOAB-2 detects preparations enriched in U-, O-, F-A?42, and U-A?40 by dot-blot, and is thus a pan-specific A? antibody. However, MOAB-2 is selective for the more neurotoxic A?42 compared to A?40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects A?40 at 2.5 pmol, but U-, O- and F-A?b42 at antigen concentrations as low as ~ 0.1 pmol (Youmans. KL et al., 2012; PMID: 22423893). MOAB-2 does not detect APP (Amyloid Precursor Protein). Human, rat, other species not yet tested. By Dot Blot, MOAB-2 detected rat A?40 and human A?40, albeit with less affinity than for A?42 (Youmans KL et al., 2012).
Storage:
After reconstitution keep aliquots at -20°C to -70°C for a higher stability. At 2-8°C keep up to one week; use sterile methods and pipettes. Highly purified glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles. Keep tightly closed when not in use and protected from light.
Purification:
Antibody was purified from cell culture supernatant by Protein G chromatography, biotinylated and buffer-exchanged into PBS, pH 7.4 buffer
The amyloid beta peptide is derived from the cleavage of the Amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. However, the form(s) of amyloid-beta peptide (A? associated with the pathology characteristic of Alzheimer's disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal A? accumulation is an area of considerable research and controversy principally because antibodies thought to be specific for A? have been shown to actually detect intraneuronal APP and not A? exclusively.<br /><br />MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 as demonstrated by biochemical and immunohistochemical analyses (IHC), and is highly specific just to amyloid beta peptide.<br /><br />MOAB-2 did not detect APP or APP-CTFs in cell culture media/lysates (HEK-APPSwe or HEK APPSwe/BACE1) or in brain homogenates from transgenic mice expressing 5 familial AD (FAD) mutation (5xFAD mice). <br /><br />Using IHC on 5xFAD brain tissue, MOAB-2 immunoreactivity co-localized with C-terminal antibodies specific for A?40 and A?42. MOAB-2 did not co-localize with either N- or C-terminal antibodies to APP. In addition, no MOAB-2-immunreactivity was observed in the brains of 5xFAD/BACE-/- mice, although significant amounts of APP were detected by N- and C-terminal antibodies to APP, as well as by 6E10.<br /><br />In both 5xFAD and 3xTg mouse brain tissue, MOAB-2 co-localized with cathepsin-D, a marker for acidic organelles, further evidence for intraneuronal A?, distinct from A? associated with the cell membrane. MOAB-2 demonstrated strong intraneuronal and extra-cellular immunoreactivity in 5xFAD and 3xTg mouse brain tissues.
Product Type:
Antibody
Antibody Type:
Monoclonal
Format:
Lyophilized, from a Protein A purified preparation in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, 0.1% trehalose, pH 7.2; contains 0.01% sodium azide as a preservative.
Host Animal:
Mouse
Species Reactivity:
Human,Rat
Immunogen:
Recombinant human amyloid beta protein 42 (A?42): DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Western Blotting (WB), Immunohistochemistry (IHC), Immunohistochemistry/paraffin embedded IH(P), Immunoprecipitation (IP), Immunofluorescence (IF), ELISA.<br><br>Antibody has been tested in WB using purified synthetic beta-amyloid preparations and from transgenic mouse brain formic acid extracts (see figure 1). Formic acid extraction/concentration is required for western blot detection from extracts. MOAB-2 antibody is specific for beta-amyloid and does not detect APP. Suggested dilution of 1:2000-1:5,000 for WB, standard ECL detection systems. <br><br>Tissue samples for the detection of beta-amyloid should be prepared as detailed in K.L. Youmans et al. {Journal of Neuroscience Methods 196 (2011) 51-59} for best results. Detection of beta-amyloid 40/42 in direct westerns can be difficult; Dot-blots of prepared samples are recommended as detailed in Youmans. KL et al 2012. <br><br>IR or fluorescent detection systems not yet tested, they but are expected to work well with higher primary antibody dilutions because of the increased sensitivity of the detection methods.<br><br>Suggested dilutions for IHC are 1:50-1:1,000. Fresh frozen, 4% paraformaldehyde fixed frozen, or formalin fixed paraffin embedded tissues are all suitable. Optimal dilutions must be determined by the end user. Antigen retrieval is required in fixed tissues for optimal staining.<br><br>Antibody was tested on 4% paraformaldehyde/0.1% glutaraldehyde fixed frozen tissue from 3xTg and 5xFAD mice. MOAB-2 antibody detects intraneuronal and extracellular beta-amyloid in IHC and does not detect APP {Youmans KL et al 2012}.<br><br> The antibody also reacts with archival formalin-fixed, paraffin-embedded tissue samples with antigen Heat Induced Epitope Retrieval (HIER): Recommended Citrate, pH 6.0 buffer for HIER. Signal was weak without antigen retrieval. Immunoreactively was expressed in intraneural-amyloid deposition (plaque) in Alzheimer's brain. MoAB-2 was found to be extremely clean and with an excellent signal to noise ratio with no neuro-cellular diffusive staining.<br><br>In addition MOAB-2 demonstrated no significant differences in A-beta detection using paraffin fixed, free-floating sections {Youmans KL et al 2012}. Formic acid (FA) treatment resulted in optimal detection of both intraneuronal and extracellular A-beta compared to without FA (incubated in 88% FA 8 min, Youmans KL et al 2012). Free floating tissue sections were permeabilized in TBS containing 0.25% Triton X-100 (TBSX; 3 x 10 min), blocked with 3% horse serum in TBSX (3 x 10 min) followed by 1% horse serum in TBSX (2 x10 min) and incubated with appropriate primary antibodies diluted in TBSX containing 1% horse serum overnight. See Youmans KL et al 2012 for full IH(P) protocol and method details.<br><br> For IF, suggested dilution is 1:100-1:500. The antibody was tested on 4% PFA fixed frozen tissue. Fixed tissues were washed in TBS (3 x 10 min), then incubated in 88% FA (8 min), and then permeabilized in TBSX (3 x 10 min), and blocked in TBSX containing 5% bovine serum albumin (BSA; 1 hr). Sections were subsequently incubated with appropriate primary antibodies diluted in TBSX containing 2% BSA overnight on an oscillatory rotator. Detection was via fluorescently labelled absorbed secondary antibodies {Youmans KL et al 2012}.<br><br>For IP, the suggested dilution is 1:200 to 1:1,000 for labeled beta-amyloid using Protein A/G conjugated beads as the capture vehicle {Youmans KL et al 2012}.<br><br>In an ELISA, a dilution of 1:50-1:1000 is suggested. The antibody has been tested in ELISAs on synthetic beta-amyloid and tissue homogenates from beta-amyloid-Tg mice. Biosensis recommends optimal dilutions/concentrations should be determined by the end user for all applications. Dilutions provided are only meant to serve as a basic guide.
Alternative Names:
Beta-APP42; Beta-APP40; Beta-amyloid protein 42; Beta-amyloid protein 40; ABPP; APPI; Amyloid beta A4 protein;MOAB2;MOAB-2; Alzheimer's antibody;AB40;AB42;abeta
Biosensis Brand:
Biosensis®
Conjugate:
Unconjugated
Shelf Life:
12 months after date of receipt (unopened vial).
Use:
For research use only.
Product references:
Setti, S.E. et al. (2022) Assessment of sex-related neuropathology and cognitive deficits in the Tg-SwDI mouse model of Alzheimers disease. Behave Brain Res. 428:113882. Application: IHC. Sil, A. et al. (2022) Sex Differences in Behavior and Molecular Pathology in the 5XFAD Model. J Alzheimers Dis. 85(2):755-778. Application: WB. Sarkar, S. et al. (2020) Modification of methods to use Congo-red stain to simultaneously visualize amyloid plaques and tangles in human and rodent brain tissue sections. Metab Brain Dis. [Epub ahead of print]. Application: IHC. Cuevas, E. et al. (2019) Amyloid Beta 25-35 induces blood-brain barrier disruption in vitro. Metab Brain Dis. [Epub ahead of print]. Application: ICC/IF. Schmued, L. et al. (2019) High Contrast and Resolution Labeling of Amyloid Plaques in Tissue Sections from APP-PS1 Mice and Humans with Alzheimer's Disease with the Zinc Chelator HQ-O: Practical and Theoretical Considerations. Curr Alzheimer Res. 16(7):577-586. Application: IHC/IF. Hui, L. et al. (2019) Acidifying Endolysosomes Prevented Low-Density Lipoprotein-Induced Amyloidogenesis. J Alzheimers Dis. 64(1):393-410. Application: ICC/IF. Koss, DJ. et al. (2018) Distinctive temporal profiles of detergent-soluble and -insoluble tau and A? species in human Alzheimer's disease. Brain Res. [Epub ahead of print]. Application: WB, dot blot. Zhao, Y. et al. (2018) TREM2 Is a Receptor for _-Amyloid that Mediates Microglial Function. Neuron. 97(5):1023-1031. Application: IHC, free-floating cryostat sections Zhu, B. et al. (2017) ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating _-secretase activity. Nat Commun. 8(1):1472. Application: IHC Huang, TY. et al. (2017) SORLA attenuates EphA4 signaling and amyloid _-induced neurodegeneration. J Exp Med. pii: jem.20171413. [Epub ahead of print]. Application: IHC Felecia, M. et al. (2017) Peripheral Inflammation, Apolipoprotein E4, and Amyloid-_ Interact to Induce Cognitive and Cerebrovascular Dysfunction. ASN Neuro. 9(4):1759091417719201. Application: IHC/IF Thomas, R. et al. (2016) Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice. Acta Neuropathol Commun. 4(1):111 Application: IHC Koster, KP. et al. (2016) Epidermal growth factor prevents oligomeric amyloid-_ induced angiogenesis deficits in vitro. J Cereb Blood Flow Metab. [Epub ahead of print] Application: IF Loffler, T. et al. (2016) Decreased Plasma A? in Hyperlipidemic APPSL Transgenic Mice Is Associated with BBB Dysfunction. Front. Neurosci. Application: IF Kobro-Flatmoen, A. et al. (2016) Reelin-immunoreactive neurons in entorhinal cortex layer II selectively express intracellular amyloid in early Alzheimer's disease. Neurobiology of Disease. 93:172-183. Application: IHC Tai, LM. et al. (2016) The role of APOE in cerebrovascular dysfunction. Acta Neuropathol. 131(5):709-23. Application: IF Kim, YH. et al. (2015) A 3D human neural cell culture system for modeling Alzheimer's disease. Nat Prot. 10(7):985-1006. Application: WB Condello, C. et al. (2015) Microglia constitute a barrier that prevents neurotoxic protofibrillar A?42 hotspots around plaques. Nat Commun. 6:6176. Application: IF Iulita MF et al (2014) Studying Alzheimer's Disease Pre-clinical Stages: Insights from Down's Syndrome and Transgenic Animal Models. PhD Thesis Application: IHC/IF Iulita MF et al (2014) Intracellular Abeta pathology and early cognitive impairments in a transgenic rat model overexpressing human amyloid precursor protein: a multidimensional study. Acta Neuropathol Commun. 6:61. Application: IF, IH Smith BR et al (2014) Neuronal inclusions of alpha-synuclein contribute to the pathogenesis of Krabbe disease. J Pathol. Apr;235(5):509-21. Application: IF
Specificity:
MOAB-2 detects preparations enriched in U-, O-, F-A?42, and U-A?40 by dot-blot, and is thus a pan-specific A? antibody. However, MOAB-2 is selective for the more neurotoxic A?42 compared to A?40. Indeed, MOAB-2 demonstrated a titration against antigen concentration, and detects A?40 at 2.5 pmol but U-, O- and FA?b42 at antigen concentrations as low as ~ 0.1 pmol {Youmans. KL et al 2012}. MOAB-2 does not detect APP (Amyloid precursor protein). Human, Rat, other species not yet tested.By Dot blot, MOAB-2 detected rat A?40 and human A?40, albeit with less affinity than for A?42. {Youmans. KL et al 2012}
Storage:
After reconstitution keep aliquots at -20 ° to -70°C for a higher stability. At 2-8°C keep up to one week, insulated, protected from light; use sterile methods and pipettes. Highly purified glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles. Keep tightly closed when not in use and protected from light.
Purification:
This product is a Protein A purified mouse IgG2b in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, 0.01% sodium azide, pH 7.2.
Rabbit anti-Amyloid-beta precursor protein (APP) Polyclonal Antibody (Unconjugated), suitable for IHC-Frozen.
Background Info:
FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Host Animal:
Rabbit
Species Reactivity:
Mouse,Rat
Immunogen:
A synthetic peptide (HMNVQNGKWESDPSGTKTC, aa: 44-62) as part of mouse APP isoform A conjugated to the immunogenic protein Blue Carrier Protein
Applications:
IHC-Frozen
Antibody Isotype:
Mixed
Application Details:
IHC. Recommended to be used at a dilution of 1:500 to 1:3000 for immunohistochemistry. This antiserum has not yet been tested for western blot. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.
Alternative Names:
Amyloid beta A4 protein; ABPP; Alzheimer disease amyloid protein homolog; Amyloidogenic glycoprotein; AG
Biosensis Brand:
Biosensis®
Conjugate:
Unconjugated
Shelf Life:
12 months after date of receipt (unopened vial).
Use:
For research use only.
Specificity:
Specificity for APP was confirmed by IHC. This antiserum is known to react with rat APP. Reactivity with other species have not yet been tested.
Storage:
After reconstitution keep aliquots at -20°C for a higher stability, and at 2-8°C with an appropriate antibacterial agent. Glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles.
Rabbit anti-Amyloid-beta precursor protein (APP) Polyclonal Antibody (Unconjugated), suitable for IHC-Frozen.
Background Info:
FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Host Animal:
Rabbit
Species Reactivity:
Human,Rat
Immunogen:
Synthetic peptides (C-ETHLHW HTVAKET, aa: 145-157; C-HAH FQKAKERLEA KHRER, aa: 388-405; C-KKKQYTS IHHGVVE, aa: 724-737) as parts of human APP isoform A conjugated to KLH
Applications:
IHC-Frozen
Antibody Isotype:
Mixed
Application Details:
IHC. Recommended to be used at a dilution of 1:500 to 1:3000 for immunohistochemistry. This antiserum has not yet been tested for western blot. Biosensis recommends optimal dilutions/concentrations should be determined by the end user.
Specificity for APP was confirmed by IHC. This antiserum is known to react with rat APP. Reactivity with other species have not yet been tested.
Storage:
After reconstitution keep aliquots at -20°C for a higher stability, and at 2-8°C with an appropriate antibacterial agent. Glycerol (1:1) may be added for an additional stability. Avoid repetitive freeze/thaw cycles.
A proprietary preparation of human amyloid beta peptide (amino acids 1-42) that was initially monomerized by HFIP-treatment and then allowed to form oligomers by the procedure described in Youmans KL et al. , 2012 , followed by lyophilisation using Biosensis' proprietary stabilization procedures. The resulting oligomeric mixture has been specially designed to allow the formation of stable, oligomeric A? 1-42 peptide, multimeric complexes or oligomers. The material is intended to be used as a stable and consistent standard or positive control for oligomeric ELISA assays, as well as other research applications.
Product Type:
Peptide
Format:
Lyophilized, Supplied as 2 x 500 ng vials, each containing lyophilized A? oligomers</b>. Note that the amount of provided oligomeric protein is based on the amount of monomeric A? used to form these oligomers. The precise formation, size and number of oligomers cannot be quantified by any known method.
Applications:
ELISA
Application Details:
<i>Use as positive control in Oligomeric A? ELISA Kit (BEK-2215)</i>: Reconstitute one vial with 1 mL of assay buffer provided in the ELISA kit. Dilute to a concentration of 0.5-1 ng/mL. At this concentration, a positive signal will be obtained within the dynamic range of the calibration curve.<br><br><i>Use as oligomeric A-beta peptide standard in Oligomeric A? ELISA Kit (BEK-2215)</i>: Reconstitute one vial with 1 mL of assay buffer provided in the ELISA kit. Dilute to a concentration of 2 ng/mL, which represents the highest concentration of the calibration curve. Perform a 1:2 serial dilution down to 0.031 ng/mL in assay buffer. Click <a class="newA" target="_blank" href="https://www.biosensis.com/documents/enhancedinfo/PE-1750-1000_Instructions for Generating a Calibration Curve.pdf"> here </a> for detailed instructions on generating a calibration curve with PE-1750-1000.<br><br><i>Use as positive control in other applications</i>: Optimal concentrations need to be determined empirically. It is recommended to reconstitute the vial with 100 - 200 µL buffer first (eg., PBS, pH 7.4), and prepare further working dilutions thereof.
Store unopened, lyophilized oligomeric A? with desiccant, insulated, at -20°C short term, -80°C long term. Store reconstituted vial at 2-8°C for up to 2 days. The reconstituted material should not be frozen for best results.
Synthetic beta-amyloid A? 1-42 was monomerized by HFIP (hexafluoro-2-propanol) treatment and dried. One vial contains 50 ?g monomeric A? peptide that can be used to form solutions of unaggregated A? monomers, aggregated A? oligomers, A? fibrils and A? protein complexes according to published protocols, and used in a variety of research applications.
Product Type:
Peptide
Format:
Lyophilized.
Applications:
ELISA
Application Details:
<i>Preparation of unaggregated A-beta<sub>1-42</sub></i>:<br><br><b>Important:</b> unaggregated A-beta has to be prepared just prior to use!<br><br>1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A-beta peptide; spin down the liquid briefly<br>2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. <b>Important</b>: refer to the attached <a class="newA" target="_blank" href="https://www.biosensis.com/documents/enhancedinfo/PE-1749-50_Peptide Reconstitution Instructions.pdf">instructions</a> for a detailed procedure to ensure that all peptide is fully reconstituted!<br>3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM. Vortex-spin for 3 more times<br> 4. Final concentration of A-beta is 450 µg/mL<br>5. Use reconstituted peptide <b>immediately</b> to avoid oligomer formation<br><br><i>Preparation of oligomeric A-beta<sub>1-42</sub></i>:<br><br>1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A-beta peptide; spin down the liquid briefly<br>2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. <b>Important</b>: refer to the attached <a class="newA" target="_blank" href="https://www.biosensis.com/documents/enhancedinfo/PE-1749-50_Peptide Reconstitution Instructions.pdf">instructions</a> for a detailed procedure to ensure that all peptide is fully reconstituted!<br>3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM<br>4. Vortex-spin for 3 more times<br>5. Incubate the solution at 2-8ºC for 24 hours (protected from light)<br>6. Final concentration of A-beta is 450 µg/mL<br>7. Once reconstituted and oligomerized, o-A-beta should be used as soon as possible and within 7 days to ensure the stability of the oligomers<br><br><b>Note:</b> while the concentration of monomeric A-beta peptide used to form the oligomeric complexes is accurately determined, the precise formation, size and number of oligomers cannot be quantified by any known method.<br><br><i>Preparation of fibrillar A-beta<sub>1-42</sub></i>:<br><br>1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A-beta peptide; spin down the liquid briefly<br>2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. <b>Important:</b> refer to the attached <a class="newA" target="_blank" href="https://www.biosensis.com/documents/enhancedinfo/PE-1749-50_Peptide Reconstitution Instructions.pdf">instructions</a> for a detailed procedure to ensure that all peptide is fully reconstituted!<br>3. Add 106 µL of 10 mM HCl to make up to 111 µL total volume and a peptide concentration of 100 µM<br>4. Vortex-spin for 3 more times<br> 5. Incubate the solution at 37ºC for 24 hours (protected from light)<br>6. Final concentration of A-beta is 450 µg/mL<br><br><i>Preparation of A-beta<sub>1-42</sub> Complexes</i>:<br><br><b>Important:</b> only unagreggated A-beta will form complexes. Use A-beta peptide immediately after reconstitution to form complexes.<br><br>1. Add 5 µL of reconstituting buffer to one vial of 50 µg of HFIP-treated A-beta peptide; spin down the liquid briefly<br>2. Vortex the vial for 5 seconds at highest speed while rotating the vial with your hands; spin down the liquid (bench-top microcentrifuge) and repeat the vortex-spin procedure for a minimum of 3 times; continue the vortex-spin procedure until all lyophilized peptide is dissolved and collected at the bottom of the tube. <b>Important:</b> refer to the attached <a class="newA" target="_blank" href="https://www.biosensis.com/documents/enhancedinfo/PE-1749-50_Peptide Reconstitution Instructions.pdf">instructions</a> for a detailed procedure to ensure that all peptide is fully reconstituted!<br>3. Add 106 µL of cold Dilution Buffer to make up to 111 µL total volume and a peptide concentration of 100 µM<br> 4. Vortex-spin for 3 more times<br> 5. Use reconstituted peptide <b>immediately</b> to avoid oligomer formation<br>6. Mix the A-beta monomer with its complex partner (eg., lipoprotein) at desired concentrations in PBS, pH 7.4, or other suitable buffers compatible with its intended application<br>7. Incubate at room temperature for 2 hours without shaking<br>8. Use complexes immediately after incubation<br><br>These protocols are based on procedures published by <a class="newA" target="_blank" href="https://www.ncbi.nlm.nih.gov/pubmed/22423893">Youmans KL <i>et al.</i>, 2012</a> and <a class="newA" target="_blank" href="https://www.ncbi.nlm.nih.gov/pubmed/23293020">Tai LM <i>et al.</i>, 2013</a>, and we refer to these publications and other relevant literature for further details.<br><br>Provided working concentrations are only meant to guide the user. Optimal concentrations depend on the experimental design and need to be determined empirically.
Biosensis is proud to offer the first commercially available ApoE/?-amyloid (ApoE/A?) complex ELISA kit. As a result of extensive collaboration with Dr. LaDu's laboratory at UIC and validation by Biosensis, this ELISA can be used to accurately and consistently measure the extent of ApoE/A? complex in tissue extracts and other samples. The Biosensis ApoE/A? Complex ELISA kit is a sandwich ELISA and consists of a pre-coated mouse monoclonal anti-A? capture antibody, a highly validated ApoE/A? complex standard that is pre-formed, lyophilized and ready for reconstitution, a biotinylated ApoE detection antibody, and horseradish peroxidase (HRP)-conjugated streptavidin and detection reagent. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the level of ApoE/A? complex present in samples and protein standards. Importantly, a well-characterized and unique ApoE/A? complex is included as a standard. This complex is pre-formed and lyophilized, requiring only reconstitution with assay diluent prior to use. In order to assess non-specific ApoE protein binding, each kit includes additional plates pre-coated with control antibody. The purpose of this kit is the in vitro qualitative measurement of ApoE/A? complexes in brain extracts and CSF samples from both transgenic mice and humans or primates, relative to a known ApoE/A? complex standard, only if used as directed. This kit has not been tested for other sample applications. This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA Assay
Species Reactivity:
Human
Immunogen:
Complex of E.coli-derived recombinant human ApoE protein and synthetic, monomerized Abeta (1-42) peptide
Applications:
ELISA
Application Details:
ELISA. For the quantification of Apolipoprotein E/beta-Amyloid Complex (ApoE/A beta) in CSF, Tissue Homogenates. Please download the detailed product insert for complete instructions for the successful use of this ELISA. Use only as directed.
The ELISA kit box contains 2 x 96-well pre-coated strip plates per 1 Plate Kit (1 plate MOAB-2 antibody coated, 1 plate control antibody coated), protein standards, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Product references:
Tai LM et al. (2013) J Biol Chem. 288(8): 5914-26 Tai LM et al. (2014) Mol Neurodegen. 9:2
Specificity:
Human Apolipoprotein E/beta-Amyloid (ApoE/A beta) Complex. The kit has been assayed on human samples only but the capture antibody, MOAB-2, is know to react with rodent amyloid beta though weaker (20% less reactivity on dot blots). The polyclonal APOE used for detection should detect ApoE from a variety of species but so far has only been tested on human
Biosensis is proud to offer the first commercially available ApoE/?-amyloid (ApoE/A?) complex ELISA kit. As a result of extensive collaboration with Dr. LaDu's laboratory at UIC and validation by Biosensis, this ELISA can be used to accurately and consistently measure the extent of ApoE/A? complex in tissue extracts and other samples. The Biosensis ApoE/A? Complex ELISA kit is a sandwich ELISA and consists of a pre-coated mouse monoclonal anti-A? capture antibody, a highly validated ApoE/A? complex standard that is pre-formed, lyophilized and ready for reconstitution, a biotinylated ApoE detection antibody, and horseradish peroxidase (HRP)-conjugated streptavidin and detection reagent. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the level of ApoE/A? complex present in samples and protein standards. Importantly, a well-characterized and unique ApoE/A? complex is included as a standard. This complex is pre-formed and lyophilized, requiring only reconstitution with assay diluent prior to use. In order to assess non-specific ApoE protein binding, each kit includes additional plates pre-coated with control antibody. The purpose of this kit is the in vitro qualitative measurement of ApoE/A? complexes in brain extracts and CSF samples from both transgenic mice and humans or primates, relative to a known ApoE/A? complex standard, only if used as directed. This kit has not been tested for other sample applications. This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA Assay
Species Reactivity:
Human
Immunogen:
Complex of E.coli-derived recombinant human ApoE protein and synthetic, monomerized Abeta (1-42) peptide
Applications:
ELISA
Application Details:
ELISA. For the quantification of Apolipoprotein E/beta-Amyloid Complex (ApoE/A beta) in CSF, Tissue Homogenates. Please download the detailed product insert for complete instructions for the successful use of this ELISA. Use only as directed.
The ELISA kit box contains 2 x 96-well pre-coated strip plates per 1 Plate Kit (1 plate MOAB-2 antibody coated, 1 plate control antibody coated), protein standards, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Product references:
Tai LM et al. (2013) J Biol Chem. 288(8): 5914-26 Tai LM et al. (2014) Mol Neurodegen. 9:2
Specificity:
Human Apolipoprotein E/beta-Amyloid (ApoE/A beta) Complex. The kit has been assayed on human samples only but the capture antibody, MOAB-2, is know to react with rodent amyloid beta though weaker (20% less reactivity on dot blots). The polyclonal APOE used for detection should detect ApoE from a variety of species but so far has only been tested on human
The oligomeric form of Amyloid Beta peptide (A?, 1-42) has been closely linked to Alzheimer's Disease. Several ELISAs targeting A? have been developed; however, these ELISAs are known to cross-react with Amyloid Beta precursor protein (APP) and are poorly characterized against monomeric and oligomeric forms of the peptide. The Biosensis MOAB-2 antibody, developed by LaDu and co-workers (Youmans K. et al. , 2012) , has been shown to specifically detect A?, but not the precursor molecule APP. When utilized in ELISAs, the oligomeric form of A? peptide (o-A?) can be assayed independently of the other forms of the molecule when assayed with the MOAB-2 monoclonal antibody. The Biosensis oligomeric A? ELISA kit is a sandwich ELISA that allows the preferential quantification of oligomeric A? peptides. This kit is exclusive to Biosensis and consists of a pre-coated mouse monoclonal anti-A? capture antibody (MOAB-2), a biotinylated MOAB-2 detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of o-A? present in samples and protein standards. The purpose of this kit is the in vitro qualitative measurement of oligomeric A? peptide levels in brain extracts and CSF samples from both transgenic mice and humans relative to a known o-A? standard. The inclusion of a highly validated oligomeric standard results in a unique, ready-to-use ELISA kit. This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA Assay
Species Reactivity:
Human,Rat
Immunogen:
The standard in this ELISA is synthetically manufactured beta-amyloid peptide, amino acids 1-42 of human, HFIP treated and dried.The stabilized oligomeric beta amyloid 1-42 control complex is also constructed from the same synthetic peptide standard material. No animal systems were used for their manufacture.
Applications:
ELISA
Application Details:
ELISA. For the quantification of Oligomeric Amyloid-beta in CSF, Tissue Homogenates. Please download the detailed product insert for complete instructions for the successful use of this ELISA. Use only as directed.
The ELISA kit box contains 96-well pre-coated strip plate(s), protein standards, QC sample, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Product references:
Kasus-Jacobi A et al. (2022) "Selecting Multitarget Peptides for Alzheimers Disease" Biomolecules. 12, 1386 Application: Human, A?142 oligomers. Eid A et al. (2022) "Effects of DDT on Amyloid Precursor Protein Levels and Amyloid Beta Pathology: Mechanistic Links to Alzheimer's Disease Risk" Environ Health Perspect. [Epub ahead of print] Application: Mouse, brain tissue homogenate. Kasus-Jacobi A et al. (2021) "Neutrophil Granule Proteins Inhibit Amyloid Beta Aggregation and Neurotoxicity." Curr Alzheimer Res. 18(5):414-427 Application: Mouse in-vitro assay, cell culture supernatant. Hark TJ et al. (2020) "Pulse-Chase Proteomics of the App Knockin Mouse Models of Alzheimer s Disease Reveals that Synaptic Dysfunction Originates in Presynaptic Terminals." Cell Syst. [Epub ahead of print] Application: Mouse cortical homogenates. Xiao L et al. (2020) "Enzyme-digested Colla Corii Asini (E'jiao) prevents hydrogen peroxide-induced cell death and accelerates amyloid beta clearance in neuronal-like PC12 cells." Neural Regen Res. 15(12): 2270-2 Application: Rat PC12 RIPA cell extract. Hrynchak MV et al. (2020) "Chronic Presence of Oligomeric A? Differentially Modulates Spine Parameters in the Hippocampus and Cortex of Mice With Low APP Transgene Expression." Front Synaptic Neurosci. Apr 24;12:16 Application: Mouse lysate. El-Sayed NA et al. (2019) "Design, synthesis, in vitro and in vivo evaluation of novel pyrrolizine-based compounds with potential activity as cholinesterase inhibitors and anti-Alzheimer's agents." Bioorg Chem. [Epub ahead of print] Application: Human. In-vitro screening of drug candidates. Oh Joo Kweon, Young Chul Youn, Yong Kwan Lim, Mi-Kyung Lee, Hye Ryoun Kim (2019) "Clinical utility of serum hepcidin and iron profile measurements in Alzheimer's disease." J Neurol Sci. [In press] Application: Human serum. Pacheco-Quinto J, Clausen D, Perez-Gonzalez R, Peng H, Meszaros A, Eckman CB, Levy E, Eckman EA (2018) "Intracellular metalloprotease activity controls intraneuronal A? aggregation and limits secretion of A? via exosomes." FASEB J. [Epub ahead of print] Application: Human cell line, mouse brain and organotypic brain slice cultures. Oh SB, Kim MS, Park S, Son H, Kim SY, Kim MS, Jo DG, Tak E, Lee JY (2018) "Clusterin contributes to early stage of Alzheimer's disease pathogenesis." Brain Pathol. [Epub ahead of print] Application: Transgenic mouse brain homogenates. S Liu, S Park, G Allington, F Prelli, Y Sun, M Marta-Ariza, H Scholtzova, G Biswas, B Brown, PB Verghese, PD Mehta, Y-U Kwon and T Wisniewski (2017) "Targeting Apolipoprotein E/Amyloid _ Binding by Peptoid CPO_A?17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline." Sci Rep. 7(1):8009 Application: Transgenic mouse brain homogenates. M Cacciottolo, X Wang, I Driscoll, N Woodward, A Saffari, J Reyes, M L Serre, W Vizuete, C Sioutas, T E Morgan, M Gatz, H C Chui, S A Shumaker, S M Resnick, M A Espeland, C E Finch and J C Chen (2017) "Particulate air pollutants, APOE alleles and their contributions to cognitive impairment in older women and to amyloidogenesis in experimental models." Transl Psychiatry. Jan 31;7(1):e1022. Application: Extracts of E3FAD and E4FAD transgenic mouse brains. Riya Thomas, Paulina Zuchowska, Alan W. J. Morris, Felecia M. Marottoli, Sangeeta Sunny, Ryan Deaton, Peter H. Gann, Leon M. Tai (2016) "Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice." Acta Neuropathol Commun. 4(1):111 Application: Tris-extracts of EFAD transgenic mouse brains. Nor Faeizah Ibrahim, Daijiro Yanagisawa, Lina Wati Durani, Hamizah Shahirah Hamezah, Hanafi Ahmad Damanhuri, Wan Zurinah Wan Ngah, Mayumi Tsuji, Yuji Kiuchi, Kenjiro Ono, Ikuo Tooyama (2016) "Tocotrienol-Rich Fraction Modulates Amyloid Pathology and Improves Cognitive Function in A?PP/PS1 Mice." J Alzheimers Dis. [Epub ahead of print]. Application: Tris-extracts of mouse brain homogenates. Jia Luo, Sue H. Lee, Lawren VandeVrede, Zhihui Qin, Manel Ben Aissa, John Larson, Andrew F. Teich, Ottavio Arancio, Yohan D'Souza, Ahmed Elharram, Kevin Koster, Leon M. Tai, Mary Jo LaDu, Brian M. Bennett and Gregory R. J. Thatcher (2016) "A multifunctional therapeutic approach to disease modification in multiple familial mouse models and a novel sporadic model of Alzheimer's disease." Molecular Neurodegeneration 2016 11:35. Application: Tris-extracts of EFAD transgenic mouse brains. Weiguo Peng, Thiyagarajan M. Achariyar, Baoman Li, Yonghong Liao, Humberto Mestre, Emi Hitomi, Sean Regan, Tristan Kasper, Sisi Peng, Fengfei Ding, Helene Benveniste, Maiken Nedergaard, Rashid Dean (2016) "Suppression of glymphatic fluid transport in a mouse model of Alzheimer's disease." Neurobiology of Disease. Vol. 93, Pages 215-225 Application: TBSX-extracts of mouse cerebral cortex. Mafalda Cacciottolo, Amy Christensen, Alexandra Moser, Jiahui Liu, Christian J. Pike, Conor Smith, Mary Jo LaDu, Patrick M. Sullivan, Todd E. Morgan, Egor Dolzhenko, Andreas Charidimou, Lars-Olof Wahlund, Maria Kristofferson Wiberg, Sara Shams, Gloria Chia-Yi Chiang (2016) "The APOE4 allele shows opposite sex bias in microbleeds and Alzheimer's disease of humans and mice." Neurobiology of Aging. Volume 37, January 2016, Pages 47-57 Application: Tris-extracts of E3FAD and E4FAD transgenic mouse brains. Combes M, Poindron P, Callizot N.(2015) "Glutamate protects neuromuscular junctions from deleterious effects of ?-amyloid peptide and conversely: An in vitro study in a nerve-muscle coculture." J Neurosci. Res. 93(4):633-43 Application: Native Rat neurites & human muscle cell co-culture supernatants. Seo, Dong Han, et al. (2015) "Plasma-enabled sustainable elemental lifecycles: honeycomb-derived graphenes for next-generation biosensors and supercapacitors." Green Chem. 17:2164-2171. Application: Synthetic constructs. Tai, LM (2014) "Amyloid-_ Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in vivo." J Biol Chem. 289(44):30538-55 Application: EFAD-Tg mice. Liu Y, Liu X, Hao W, Decker Y, Schomburg R, Fulop L, Pasparakis M, Menger MD, Fassbender K. (2014) "IKKbeta Deficiency in Myeloid Cells Ameliorates Alzheimer's Disease-Related Symptoms and Pathology." (2014) J Neurosci. Sep 24;34(39):12982-99 Application: Transgenic Mouse brain lysates, supernatants.
Specificity:
Human. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 and is highly specific just to amyloid beta peptide. The Biosensis o-A? Elisa detects A? oligomers as validated and described by Youmans KL et al (2012) and Rat by Combes M et al (2015). Rat.
The oligomeric form of Amyloid Beta peptide (A?, 1-42) has been closely linked to Alzheimer's Disease. Several ELISAs targeting A? have been developed; however, these ELISAs are known to cross-react with Amyloid Beta precursor protein (APP) and are poorly characterized against monomeric and oligomeric forms of the peptide. The Biosensis MOAB-2 antibody, developed by LaDu and co-workers (Youmans K. et al. , 2012) , has been shown to specifically detect A?, but not the precursor molecule APP. When utilized in ELISAs, the oligomeric form of A? peptide (o-A?) can be assayed independently of the other forms of the molecule when assayed with the MOAB-2 monoclonal antibody. The Biosensis oligomeric A? ELISA kit is a sandwich ELISA that allows the preferential quantification of oligomeric A? peptides. This kit is exclusive to Biosensis and consists of a pre-coated mouse monoclonal anti-A? capture antibody (MOAB-2), a biotinylated MOAB-2 detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of o-A? present in samples and protein standards. The purpose of this kit is the in vitro qualitative measurement of oligomeric A? peptide levels in brain extracts and CSF samples from both transgenic mice and humans relative to a known o-A? standard. The inclusion of a highly validated oligomeric standard results in a unique, ready-to-use ELISA kit. This kit has been configured for research use only and is not to be used in diagnostic or clinical procedures.
Product Type:
ELISA Assay
Species Reactivity:
Human,Rat
Immunogen:
The standard in this ELISA is synthetically manufactured beta-amyloid peptide, amino acids 1-42 of human, HFIP treated and dried.The stabilized oligomeric beta amyloid 1-42 control complex is also constructed from the same synthetic peptide standard material. No animal systems were used for their manufacture.
Applications:
ELISA
Application Details:
ELISA. For the quantification of Oligomeric Amyloid-beta in CSF, Tissue Homogenates. Please download the detailed product insert for complete instructions for the successful use of this ELISA. Use only as directed.
The ELISA kit box contains 96-well pre-coated strip plate(s), protein standards, QC sample, detection reagents, wash and sample buffers, substrate buffer and detailed protocols.
Product references:
Kasus-Jacobi A et al. (2022) "Selecting Multitarget Peptides for Alzheimers Disease" Biomolecules. 12, 1386 Application: Human, A?142 oligomers. Eid A et al. (2022) "Effects of DDT on Amyloid Precursor Protein Levels and Amyloid Beta Pathology: Mechanistic Links to Alzheimer's Disease Risk" Environ Health Perspect. [Epub ahead of print] Application: Mouse, brain tissue homogenate. Kasus-Jacobi A et al. (2021) "Neutrophil Granule Proteins Inhibit Amyloid Beta Aggregation and Neurotoxicity." Curr Alzheimer Res. 18(5):414-427 Application: Mouse in-vitro assay, cell culture supernatant. Hark TJ et al. (2020) "Pulse-Chase Proteomics of the App Knockin Mouse Models of Alzheimer s Disease Reveals that Synaptic Dysfunction Originates in Presynaptic Terminals." Cell Syst. [Epub ahead of print] Application: Mouse cortical homogenates. Xiao L et al. (2020) "Enzyme-digested Colla Corii Asini (E'jiao) prevents hydrogen peroxide-induced cell death and accelerates amyloid beta clearance in neuronal-like PC12 cells." Neural Regen Res. 15(12): 2270-2 Application: Rat PC12 RIPA cell extract. Hrynchak MV et al. (2020) "Chronic Presence of Oligomeric A? Differentially Modulates Spine Parameters in the Hippocampus and Cortex of Mice With Low APP Transgene Expression." Front Synaptic Neurosci. Apr 24;12:16 Application: Mouse lysate. El-Sayed NA et al. (2019) "Design, synthesis, in vitro and in vivo evaluation of novel pyrrolizine-based compounds with potential activity as cholinesterase inhibitors and anti-Alzheimer's agents." Bioorg Chem. [Epub ahead of print] Application: Human. In-vitro screening of drug candidates. Oh Joo Kweon, Young Chul Youn, Yong Kwan Lim, Mi-Kyung Lee, Hye Ryoun Kim (2019) "Clinical utility of serum hepcidin and iron profile measurements in Alzheimer's disease." J Neurol Sci. [In press] Application: Human serum. Pacheco-Quinto J, Clausen D, Perez-Gonzalez R, Peng H, Meszaros A, Eckman CB, Levy E, Eckman EA (2018) "Intracellular metalloprotease activity controls intraneuronal A? aggregation and limits secretion of A? via exosomes." FASEB J. [Epub ahead of print] Application: Human cell line, mouse brain and organotypic brain slice cultures. Oh SB, Kim MS, Park S, Son H, Kim SY, Kim MS, Jo DG, Tak E, Lee JY (2018) "Clusterin contributes to early stage of Alzheimer's disease pathogenesis." Brain Pathol. [Epub ahead of print] Application: Transgenic mouse brain homogenates. S Liu, S Park, G Allington, F Prelli, Y Sun, M Marta-Ariza, H Scholtzova, G Biswas, B Brown, PB Verghese, PD Mehta, Y-U Kwon and T Wisniewski (2017) "Targeting Apolipoprotein E/Amyloid _ Binding by Peptoid CPO_A?17-21 P Ameliorates Alzheimer's Disease Related Pathology and Cognitive Decline." Sci Rep. 7(1):8009 Application: Transgenic mouse brain homogenates. M Cacciottolo, X Wang, I Driscoll, N Woodward, A Saffari, J Reyes, M L Serre, W Vizuete, C Sioutas, T E Morgan, M Gatz, H C Chui, S A Shumaker, S M Resnick, M A Espeland, C E Finch and J C Chen (2017) "Particulate air pollutants, APOE alleles and their contributions to cognitive impairment in older women and to amyloidogenesis in experimental models." Transl Psychiatry. Jan 31;7(1):e1022. Application: Extracts of E3FAD and E4FAD transgenic mouse brains. Riya Thomas, Paulina Zuchowska, Alan W. J. Morris, Felecia M. Marottoli, Sangeeta Sunny, Ryan Deaton, Peter H. Gann, Leon M. Tai (2016) "Epidermal growth factor prevents APOE4 and amyloid-beta-induced cognitive and cerebrovascular deficits in female mice." Acta Neuropathol Commun. 4(1):111 Application: Tris-extracts of EFAD transgenic mouse brains. Nor Faeizah Ibrahim, Daijiro Yanagisawa, Lina Wati Durani, Hamizah Shahirah Hamezah, Hanafi Ahmad Damanhuri, Wan Zurinah Wan Ngah, Mayumi Tsuji, Yuji Kiuchi, Kenjiro Ono, Ikuo Tooyama (2016) "Tocotrienol-Rich Fraction Modulates Amyloid Pathology and Improves Cognitive Function in A?PP/PS1 Mice." J Alzheimers Dis. [Epub ahead of print]. Application: Tris-extracts of mouse brain homogenates. Jia Luo, Sue H. Lee, Lawren VandeVrede, Zhihui Qin, Manel Ben Aissa, John Larson, Andrew F. Teich, Ottavio Arancio, Yohan D'Souza, Ahmed Elharram, Kevin Koster, Leon M. Tai, Mary Jo LaDu, Brian M. Bennett and Gregory R. J. Thatcher (2016) "A multifunctional therapeutic approach to disease modification in multiple familial mouse models and a novel sporadic model of Alzheimer's disease." Molecular Neurodegeneration 2016 11:35. Application: Tris-extracts of EFAD transgenic mouse brains. Weiguo Peng, Thiyagarajan M. Achariyar, Baoman Li, Yonghong Liao, Humberto Mestre, Emi Hitomi, Sean Regan, Tristan Kasper, Sisi Peng, Fengfei Ding, Helene Benveniste, Maiken Nedergaard, Rashid Dean (2016) "Suppression of glymphatic fluid transport in a mouse model of Alzheimer's disease." Neurobiology of Disease. Vol. 93, Pages 215-225 Application: TBSX-extracts of mouse cerebral cortex. Mafalda Cacciottolo, Amy Christensen, Alexandra Moser, Jiahui Liu, Christian J. Pike, Conor Smith, Mary Jo LaDu, Patrick M. Sullivan, Todd E. Morgan, Egor Dolzhenko, Andreas Charidimou, Lars-Olof Wahlund, Maria Kristofferson Wiberg, Sara Shams, Gloria Chia-Yi Chiang (2016) "The APOE4 allele shows opposite sex bias in microbleeds and Alzheimer's disease of humans and mice." Neurobiology of Aging. Volume 37, January 2016, Pages 47-57 Application: Tris-extracts of E3FAD and E4FAD transgenic mouse brains. Combes M, Poindron P, Callizot N.(2015) "Glutamate protects neuromuscular junctions from deleterious effects of ?-amyloid peptide and conversely: An in vitro study in a nerve-muscle coculture." J Neurosci. Res. 93(4):633-43 Application: Native Rat neurites & human muscle cell co-culture supernatants. Seo, Dong Han, et al. (2015) "Plasma-enabled sustainable elemental lifecycles: honeycomb-derived graphenes for next-generation biosensors and supercapacitors." Green Chem. 17:2164-2171. Application: Synthetic constructs. Tai, LM (2014) "Amyloid-_ Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in vivo." J Biol Chem. 289(44):30538-55 Application: EFAD-Tg mice. Liu Y, Liu X, Hao W, Decker Y, Schomburg R, Fulop L, Pasparakis M, Menger MD, Fassbender K. (2014) "IKKbeta Deficiency in Myeloid Cells Ameliorates Alzheimer's Disease-Related Symptoms and Pathology." (2014) J Neurosci. Sep 24;34(39):12982-99 Application: Transgenic Mouse brain lysates, supernatants.
Specificity:
Human. MOAB-2 (mouse IgG2b) is a pan-specific, high-titer antibody to A? residues 1-4 and is highly specific just to amyloid beta peptide.The Biosensis o-A? Elisa detects A? oligomers as validated and described by Youmans KL et al (2012) and Rat by Combes M et al (2015). Rat.
Storage:
Store at 2-8°C
Range:
0.031 - 2 ng/mL
Sample Type:
CSF,Tissue Homogenates
Target:
Oligomeric Amyloid-beta
Uniprot Number:
P05067
Cookies:
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