The catenins, (alpha, beta and gamma) are cytoplasmic proteins which bind to the highly conserved tail of the E-cadherin molecule. Beta-catenin is a component of the adherens junction, a multiprotein complex which supports Ca2+ -dependent cell-to-cell contact, which in itself is critical for adhesion, signal transmission and for anchoring the actin cytoskeleton. Beta-catenin's role is as a transcription effector of the wnt-signaling pathway. Immunohistochemistry is the best way to demonstrate nuclear expression of beta-catenin and wnt-pathway activation. This aberrant expression is observed in human tumorigenesis, and especially in colorectal cancer.
Antibody Isotype:
IgG2a
Monosan Range:
MONXtra
Clone:
17C2
Concentration:
Greater than or equal to 51 mg/L
Storage buffer:
Tissue culture supernatant with sodium azide
Storage:
2-8°C
References 1:
Curia MC et al. Modern Pathology. 2008; 21:7-14
References 2:
Ortega P et al. Clinical Cancer Research. 2008; 14(14):995-1001
References 3:
Daa T et al. J. of Exp.Clin.Cancer Research. 2005; 24(1):83-87
References 4:
Fadare O et al. World Journal of Surgical Oncology. 2005; 3(38)
References 5:
Gamachi A et al.Modern Pathology. 2003; 16(11):1124-1131
The monoclonal antibody recognizes rat CD8 antigen (MW 34 kDa and 39 kDa) and is reactive with all common inbred strains. 15-11C5 is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from Balb/c mice immunized with WAG/Rij spleen cells.
The monoclonal antibody 5G5 reacts with the Toll-like receptor 9 (TLR9, CD289). TLRs are highly conserved throughout evolution and have been implicated in the innate defence to many pathogens. In Drosophila, toll is required for the anti-fungal response, while the related 18-wheeler is involved in antibacterial defences. In mammals, TLRs identified as type I transmembrane signalling receptors with pattern recognition capabilities, have been implicated in the innate host defence to pathogens. As investigated so far all functional characterized TLR signal via the TLR/IL-1 receptor (IL-1R) pathway where recruitment of MyD88 seems to be essential. In contrast to cell-wall components, bacterial DNA is probably invisible for immune cells until DNA is liberated during processes taking place in the endosomal/lysosomal compartment where intracellular TLR9 recruits MyD88 to initiate signal transduction. Unmethylated CpG-dinucleotide-containing sequences are found much more frequently in bacterial genomes than in vertebrates genomes, whereas the frequency of CpG dinucleotides are suppressed and usually methylated. The regions adjacent to the CpG dinucleotides also affect the immunostimulatory activity. The optimal sequence differs significantly between mammalian species. Methylated CpG dinucleotides lack immunostimulatory activities. Cellular activation in response to bacterial DNA and synthetic dinucleotides containing unmethylated CpG-dinucleotides is mediated by TLR9. The monoclonal antibody 5G5 reacts with RAW macrophages and TLR9 transfected HEK293 cells, and it is cross reactive with canine TLR9.
Antibody Isotype:
IgG2a
Monosan Range:
MONOSAN
Clone:
5G5
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Ahmad-Nejad; P et al. Eur J Immunol 2002; 32: 1958
The monoclonal antibody 5G5 recognizes human Toll-like receptor 9. Toll-like receptors (TLRs) are highly conserved from Drosophila to humans and share structural and functional similarities. TLRs constitute of a family of pattern recognition receptors (PRRs) that mediate cellular responses to a large variety of pathogens (viruses, bacteria, and parasites) by specific recognition of so-called âpathogen-associated molecular patternsâ. Activation of TLRs, a family of at least 11 differentmembers that function either as homo- or heterodimers, leads to activation of NFκB-dependent and IFNregulatory factor-dependent signaling pathways. TLRs have a central role in innate immunity and are also required for the development of an adaptive immune response. TLRs are expressed by various cells of the immune system, such as macrophages and dendritic cells. They recognize and respond to molecules derived from bacterial, viral and fungal pathogens.<br /> Whereas most TLRs are expressed on the cell surface, TLR9 is expressed intracellularly within one or more endosomal compartments and recognizes nucleic acids. TLR9 detects a rather subtle difference in the DNA of vertebrates compared with that of pathogens. Vertebrate genomic DNAs have mostly methylated CpG dinucleotides where bacterial and viral DNAs have unmethylated CpG dinucleotides. TLR9 undergoes relocation from endoplasmic reticulum to CpG-ODN-containing endosomes. In these endosomes TLR9 becomes a functional receptor after proteolytic cleavage. TLR9 exists as a preformed homodimer and CpG-ODN binding promotes its conformational change, bringing the cytoplasmic TIR-like domains close to each other. This allows a recruitment of the key adapter protein MyD88 which initiates a signalling cascade. The only human immune cell types known to constitutively express TLR9 and to be activated by CpG ODN are pDCs and B cells. TLR9 triggering induces an activation phenotype in the B cells and pDCs, characterized by the expression of costimulatory molecules, resistance to apoptosis, and induces Th1-type immune response profiles.
Antibody Isotype:
IgG2a
Monosan Range:
MONOSAN
Clone:
5G5
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Ahmad-Nejad; P et al. Eur J Immunol 2002; 32: 1958
The monoclonal antibody M.Ab.F11 recognizes junctional adhesion molecule-A (JAM-A) also known as the human platelet F11-Receptor (F11R) or JAM-1. JAM-A is a surface glycoprotein duplex (32 and 35 kDa) belongingto the immunoglobulin superfamily found on the surface of human platelets and at intercellular junctions of endothelial cells and epithelial cells. JAM-A belongs together with JAM-C (JAM-2) and JAM-B (VE-JAM or JAM-3) to a family of adhesion proteins with a V-C2 immunoglobulin domain organization. JAM-A plays an important role in tight junctions where it is involved in cell-to-cell adhesion through homophilic interactions. It co-distributes with other tight junction components such as ZO-1, 7H6 antigen, cingulin and occludin. Moreover, JAM-A plays a role in platelet aggregation, secretion, adhesion, spreading.<br /> In the platelet, JAM-A is a membrane protein involved in 2 distinct processes initiated on the platelet surface. Namely,, antibody-induced platelet aggregation and secretion both dependent on FcgammaRII and GPIIb/IIIa integrin, a process that may be involved in pathophysiological processes associated with certain thrombocytopenias and secondly, antibody mediated platelet adhesion independent from FcgammaRII or- fibrinogen receptor that appears to play a role in physiological processes associated with platelet adhesion and aggregation. A physiological role for the JAM-A protein was demonstrated by its phosphorylation after the stimulation of platelets by thrombin and collagen. A pathophysiological role for the JAM-A was revealed by demonstrating the presence of JAM-A antibodies in patients with thrombocytopenia. Adhesion of platelets through JAM-A resulted in events characteristic of the action of cell adhesion molecules. Recent data suggests a role for JAM-A in the adhesion of platelets to cytokine-inflamed endothelial cells and thus in thrombosis and atherosclerosis induced in non-denuded blood vessels by inflammatory processes.
SV40, Simian Virus 40 is a polyomavirus that is found in both monkeys and humans. Like other polyomaviruses, SV40 is a DNA virus that has the potential to cause tumors. SV40 is believed to suppress the transcriptional properties of tumor-suppressing p53 in humans through the SV40 large T-antigen and SV40 small T-antigen. It is generally assumed that large T-antigen is the major protein involved in neoplastic processes and the large T-antigen predominantly exerts its effect through deregulation of tumor suppressor p53, which is responsible for initiating regulated cell death (apoptosis), or cell cycle arrest when a cell is damaged. A mutated p53 gene may contribute to uncontrolled cellular proliferation, leading to a tumor.
Antibody Isotype:
IgG2a
Monosan Range:
MONOSAN
Clone:
MRQ-4
Concentration:
n/a
Storage buffer:
Tris Buffer, pH 7.3-7.7, containing 1% BSA and <0.1% Sodium Azide
Storage:
2-8°C
References 1:
Gurney, E.G., et al. J Virl. 34:752-763 (1980)
References 2:
Huang, H., Reis,R. et al. Brain Pathol., 9:33-42 (1999)
References 3:
Arrington, A.S., et al. Molecular and Clinical Perspectives; 461-489 (2001)
T-cell leukemia/lymphoma protein 1 (TCL1, TCL1A, p14TCL1) is a 14 kDa product of the TCL1 gene that is involved in T-cell prolymphocytic leukemia (T-PLL). TCL1 protein is normally found in the nucleus and cytoplasm of lymphoid lineage cells during early embryogenesis. TCL1 is expressed in differentiated Bcells under both reactive and neoplastic conditions, antigen committed B-cells, and in germinal center B-cells. The Anti-TCL1 immunohistochemical reactivity is reportedly useful identifying B-cell lymphomas including follicular lymphoma and Burkitt lymphoma.
Antibody Isotype:
IgG
Monosan Range:
MONOSAN
Clone:
MRQ-7
Concentration:
n/a
Storage buffer:
Tris Buffer, pH 7.3-7.7, containing 1% BSA and <0.1% Sodium Azide
Storage:
2-8°C
References 1:
Takizawa J, et al. Jpn J Cancer Res. 1998; 89:712-8
References 2:
Narducci MG, et al. Cancer Res. 2000; 60:2095-100
References 3:
Rodig SJ, et al. Am J Surg Pathol. 2008; 32:113-22
References 4:
Herling M, et al. Leukemia. 2006; 20:280-5
References 5:
Pescarmona E, et al. Histopathology. 2006; 49:343-8
The monoclonal antibody DCN47.5 reacts with the C-type lectin, DC-SIGN (CD209), exclusively expressed on human dendritic cells (DC). DC are specialized antigen presenting cells and bridge the innate and the adaptive immune system. They provide high levels of costimulation necessary for activation of both naïve and antigen-experienced T-cells. Immature DC are capable to migrate to inflammatory sites, capture antigen and process it internally to form MHC-peptide complexes. Following antigen uptake, DC undergo maturation and migrate to lymphoid organs where they can present MHC-peptide complexes to resting T-cells and drive T-cell proliferation. During differentiation and maturation of DC, several phenotypic surface markers are expressed: CD1a, CD4, CD11, CD40, CD86, and HLA-DR. Immature DC predominantly express CCR5 which enables DC to migrate to inflammatory sites, whereas mature DC express high levels of CXCR4, a receptor that facilitates migration to lymphoid organs.</br> DC also express DC-specific, ICAM-3 grabbing, nonintegrin (DC-SIGN), a 44 kDa C-type lectin that binds to the HIV-1 envelope glycoprotein gp120, ICAM-3 on T-cells and ICAM-2 on endothelial cells. HIV virions are able to infect cells expressing CD4 and the chemokine co-receptors CCR5 or CXCR4 and can attach to DC-SIGN to extend virion lifespan. Therefore, DC are candidates for HIV-1 infection. DC-SIGN-ICAM-3 binding is integrin-independent but calcium-dependent and antibodies reactive against DC-SIGN can be used to study DC-SIGN-ICAM3 binding.</br> The monoclonal antibody DCN47.5 specifically reacts with the C-type lectin DC-SIGN (CD209) expressed on human dendritic cells and inhibits binding of DC-SIGN to ICAM-2 on endothelial cells.
This antibody stains a minority of primary melanomas and half of the metastatic lesions tested. It rarely stains dysplastic naevi or common cellular naevi using standard immunohistochemical conditions. The antibody recognizes two protein bands in immunoblotting with a molecular weight of 95-100 kD.
Antibody Isotype:
IgG1
Monosan Range:
MONOSAN
Clone:
PAL-M2
Concentration:
10 ug/ml
Storage buffer:
Culture medium with 0.01M Sodium Azide
Storage:
2-8°C
References 1:
Ruiter DJ et al., (1985) J Invest Dermatol 85, 4-8
The monoclonal antibody 4H5 reacts specifically with full length human natural and recombinant Bactericidal Permeability Increasing protein (BPI). The antimicrobial protein BPI is a 55 kDa protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airways disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21 kDa bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage against invasive pneumococcal disease by binding to the gram-positive bacterial pathogen, pneumolysin. The monoclonal antibody 4H5 recognizes only free BPI and does not interact with BPI that has formed a complex with LPS.
The antibody reacts with the ?? subunit of the integrin protein family and seems to be human specific. The antibody reacts with an extracellular epitope of the ?? integrin molecule. Mab DF5 does react with paraffin sections
The monoclonal antibody T2.5 recognizes human Toll-like receptor 2 (TLR2). Toll-like receptors (TLR) are highly conserved throughout evolution and have been implicated in the innate defense to many pathogens. At present, ligands for several of the TLR's, such as TLR2-6,9, have been identified, confirming their role in first line defense against invading microorganism. In mammals, TLRs are identified as type I transmembrane signaling receptors with an extracellular portion containing leucine-rich repeats with pattern recognition capabilities. Pathogen recognition by TLRs provokes rapid activation of innate immunity by inducing proliferation of proinflammatory cytokines and upregulation of costimulatory molecules and eventually toinitiation of adaptive immunity. TLR2 has been identified as a receptor that is central to the innate immune response to lipoproteins of Gram-negative bacteria, several whole Gram-positive bacteria, as well as a receptor for peptidoglycan and lipoteichoic acid and other bacterial cell membrane products. It is suggested that TLR2 is able to recognize such a wide variety of PAMPs (pathogen-specific molecular patterns) by forming heterodimers with other TLRs like e.g. TLR6. TLR2 is essential for recognizing lipopeptides and lipoproteins from several microorganisms and also peptidoglycans derived from gram-positive bacteria. Bacterial species as diverse as mycobacteria, spirochetes, mycoplasma, Staphylococcus aureus, and Streptococcus pneumoniae have all been shown to mediate cellular activation via TLR2.
Toll-like receptors (TLRs) are highly conserved from Drosophila to humans and share structural and functional similarities. TLRs constitute of a family of pattern recognition receptors (PRRs) that mediate cellular responses to a large variety of pathogens (viruses, bacteria, and parasites) by specific recognition of so-called âpathogen-associated molecular patternsâ. Activation of TLRs, a family of at least 11 different members that function either as homo- or heterodimers, leads to activation of NFκB-dependent and IFN-regulatory factor-dependent signaling pathways. TLRs have a central role in innate immunity and are also required for the development of an adaptive immune response. TLRs are expressed by various cells of the immune system, such as macrophages and dendritic cells. TLRs are class I receptors, with a single ?-helix that spans the cell membrane. They recognize and respond to molecules derived from bacterial, viral and fungal pathogens, such as lipopolysaccharide (LPS) from the outer membrane of Gram negative bacteria, peptidoglycan fragments from bacterial cell walls and single-stranded and double-stranded RNA from viruses. Toll-like receptor 4 (TLR4; CD284) has been identified, next to MD-2 and CD14, as a receptor that is central to the innate immune response to LPS of Gram-negative bacteria. TLR4 is unique among TLRs in its ability to activate two distinct signaling pathways; one pathway is activated by the adaptors TIRAP (Toll/interleukin-1- receptor (TIR)-domain-containing adaptor protein) and MyD88, which leads to the induction of proâinflammatory cytokines. The second pathway is activated by the adaptors TRIF (TIR-domaincontaining adaptor protein inducing interferonâβ) and TRAM (TRIFrelated adaptor molecule), which leads to the induction of type I interferons. The monoclonal antibody HTA125 is a TLR4 function-blocking antibody. HTA125 recognizes preferentially human TLR4 that is associated with MD-2.
Antibody Isotype:
IgG2a
Monosan Range:
MONOSAN
Clone:
HTA125
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Shimazu; R et al. J Exp Med 1999; 189: 1777
References 2:
Tabeta, K et al Infect Immun 2000, 68: 3731
References 3:
Akashi; S et al. Biochem Biophys Res Commun 2000; 268: 172
The antibody reacts specificly with Human IL-1RII. The IL-1 system includes two agonists (IL-1alpha and IL-1beta), converting enzymes, antagonists, two receptors (IL-1RI and IL-1RII) and the IL-1 receptor accessory protein. The IL-1RII is part of the antagonistic IL-1 mechanism. It is also known as decoy receptor and is a non signaling molecule which functions by capturing IL-1 and preventing it from interacting with the signalling IL-1RI. The decoy IL-1RII can after binding to IL-1 also recruit the IL-1 receptor accessory protein and thus inhibit by coreceptor competition. Further a soluble form of IL-1RII exists which is shed, a process in which matrix metalloproteases have been found to play a role, by various cells including monocytes, polymorphonuclear cells, B cells and fibroblasts.
Antibody Isotype:
IgG1
Monosan Range:
MONOSAN
Clone:
8.5
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Mantovani; A et al. Ann N Y Acad Sci 1998; 840: 338
The antibody reacts specificly with Human IL-1RII. The IL-1 system includes two agonists (IL-1alpha and IL-1beta), converting enzymes, antagonists, two receptors (IL-1RI and IL-1RII) and the IL-1 receptor accessory protein. The IL-1RII is part of the antagonistic IL-1 mechanism. It is also known as decoy receptor and is a non signaling molecule which functions by capturing IL-1 and preventing it from interacting with the signalling IL-1RI. The decoy IL-1RII can after binding to IL-1 also recruit the IL-1 receptor accessory protein and thus inhibit by coreceptor competition. Further a soluble form of IL-1RII exists which is shed, a process in which matrix metalloproteases have been found to play a role, by various cells including monocytes, polymorphonuclear cells, B cells and fibroblasts.
Antibody Isotype:
IgG2a
Monosan Range:
MONOSAN
Clone:
6G5
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Mantovani; A et al. Ann N Y Acad Sci 1998; 840: 338
One of the several classes of mitochondrial proteases is membrane bound, ATPdependent FtsH protease. Their function is very important for the control of protein quality and quantity by degradation of unassembled subunits. Other names: AtFtsH3, cell division protease ftsH homolog 3, mitochondrial, AtFtsH10, cell division protease ftsH homolog 10, mitochondrial
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20 °C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Host Animal:
Rabbit
Species Reactivity:
Arabidopsis thaliana
Expected Species:
Arabidopsis thaliana
Immunogen:
KLH-conjugated peptide dereived from sequences of Arabidopsis thaliana FtsH3 and FtsH10 with localization to mitochondria Q84WU8, At2g29080 and Q8VZI8, At1g07510
No confirmed exceptions from predicted reactivity are currently known
Selected references:
Kolodziejczak et al. (2018). m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation. Plant Cell Physiol. 2018 May 1;59(5):1006-1016. doi: 10.1093/pcp/pcy041.Piechota et al. (2010). Identification and characetization of high-molecular-weight complexes fromed by m-AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana. J Biol Chem. 2010 Apr 23;285(17):12512-21. doi: 10.1074/jbc.M109.063644.
Special application note:
Blue-native (2D BN/SDS-PAGE) methodology is described in Piechota et al. 2010
One of the several classes of mitochondrial proteases is membrane bound, ATP dependent FtsH protease. Their function is very important for the control of protein quality and quantity by degradation of unassembled subunits. FtsH10 is localized in mitochondria. Alternative names: cell division protease ftsH homolog 10, mitochondrial, AtFtsH10
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20 °C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Host Animal:
Rabbit
Species Reactivity:
Arabidopsis thaliana
Expected Species:
Arabidopsis thaliana
Immunogen:
KLH-conjugated peptide located near C-terminus chosen from sequence of Arabidopsis thaliana FtsH10 Q8VZI8, At1g07510
Applications:
Blue Native PAGE (BN-PAGE), Immunoprecipitation (IP)
No confirmed exceptions from predicted reactivity are currently known
Selected references:
Kolodziejczak et al. (2018). m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation. Plant Cell Physiol. 2018 May 1;59(5):1006-1016. doi: 10.1093/pcp/pcy041.Piechota et al. (2015). Unraveling the functions of type II-prohibitins in Arabidopsis mitochondria. Plant Mol Biol. 2015 Apr 21.Kwasniak et al. (2013). Silencing of the Nuclear RPS10 Gene Encoding Mitochondrial Ribosomal Protein Alters Translation in Arabidiopsis Mitochondria. Plant Cell, May 30.Quesada et al. (2011). Arabidopsis RUGOSA2 encodes an mTERF family member required for mitochondrion, chloroplast and leaf development. Plant J.
Special application note:
Blue-native (2D BN/SDS-PAGE) methodology has been described in Piechota et al, 2010
Our purified lyophilized exosomes are obtained from different biological sources including cell culture supernatant, human plasma, serum and urine. Isolation is performed by a combination of ultracentrifugation and microfiltration procedures, and subsequent quantification/validation for overall protein content and particle number by NTA with Nanosight.
Background Info:
Exosomes are small endosome derived lipid nanoparticles (50-120 nm) actively secreted by exocytosis by most living cells. Exosome release occurs either constitutively or upon induction, under both normal and pathological conditions, in a dynamic, regulated and functionally relevant manner. Both amount and molecular composition of released exosomes depend on the state of a parent cell. Exosomes have been isolated from diverse cell lines (hematopoietic cells, tumor lines, primary cultures, virus infected cells) as well as from biological fluids in particular blood (e.g. serum and plasma from cancer patients) and other body fluids (bronchoalveolar lavage fluid, pleural effusions, synovial fluid, urine, amniotic fluid, semen, saliva etc). Exosomes have pleiotropic physiological and pathological functions and an emerging role in diverse pathological conditions such as cancer, infectious and neurodegenerative diseases.
Product Type:
Lyophilized exosomes
Storage Temp:
Store up to 3 years at 4°C >>> Storage of reconstituted exosomes: -20°C for up to one month or -80°C for up to 6 months. Avoid repeated freeze-and-thaw cycles.
Lyophilization is an ideal method for long-term storage of exosomes and microvesicles. It does not alter the stability of exosome proteins and nucleic acids, in comparison to other storage methods, including storage of fresh EVs at -20°C. Lyophilized EVs and microvesicles are easy to ship and stable for long term storage (up to 36 months).
Application Details:
Assay calibration. Control (spike-in) for exosome quantification. Protein marker analysis using different techniques. Extraction and analysis of exosome nucleic acid. Standardized positive controls for immunocapture performance evaluation. Flow cytometry. Electron microscopy.
Plant NADH dependent isocitrate dehydrogenase enzyme is located in mitochondrial matrix. This enzyme is classified as an oxidoreductase and its function is to catalyze a reaction in the citric acid cycle, specifically the sequential dehydrogenation and decarboxylation of isocitrate to form a-ketoglutarate. It removes hydrogens from its substrate, isocitrate. In addition to this process, it functions as a decarboxylase, removing a CO2 from the six-carbon substrate to form a five-carbon product mentioned above as a-ketoglutarate. There are two forms of this enzyme NADP+ and NAD+ dependent.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20 °C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Brachypodium distachyon, Brassica napus, Capsella rubella, Citrus sinensis, Glycine max, Hordeum vulgare, Malus x domestica, Medicago truncatula, Nicotiana tabacum, Phaseolus vulgaris, Theobroma cacao, Triticum aestivum, Vitis vinifera, Zea mays Species of your interest not listed? Contact us
Immunogen:
KLH-conjugated peptide 1 and peptide 2 conserved in all higher plants mitochondrial, NAD dependent isocitrate dehydrogenase subunits including Arabidopsis thaliana IDH-I Q8LFC0, At4g35260 and IDH-II P93032, At2g17130
Cellular [compartment marker] of mitochondrial matrix
Application Details:
1:400 (IF), 1 : 5 000 (WB)
Purity:
Immunogen affinity purified serum in PBS pH 7.4.
Reconstitution:
For reconstitution add 50 l of sterile water
Molecular Weight:
39 | 45 kDa (Arabidopsis thaliana)
Not reactive in:
Chlamydomonas reinhardtii
Selected references:
Kolodziejczak et al. (2018). m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation. Plant Cell Physiol. 2018 May 1;59(5):1006-1016. doi: 10.1093/pcp/pcy041.Rurek et al. (2018). Mitochondrial Biogenesis in Diverse Cauliflower Cultivars under Mild and Severe Drought Involves Impaired Coordination of Transcriptomic and Proteomic Response and Regulation of Various Multifunctional Proteins. Preprints 2018, 2018010276 (doi: 10.20944/preprints201801.0276.v1).Fujii et al. (2016). The Restorer-of-fertility-like 2 pentatricopeptide repeat protein and RNase P are required for the processing of mitochondrial orf291 RNA in Arabidopsis. Plant J. 2016 Jun;86(6):504-13. doi: 10.1111/tpj.13185.Yin et al. (2016). Comprehensive Mitochondrial Metabolic Shift during the Critical Node of Seed Ageing in Rice. PLoS One. 2016 Apr 28;11(4):e0148013. doi: 10.1371/journal.pone.0148013. eCollection 2016.Rurek et al. (2015). Biogenesis of mitochondria in cauliflower (Brassica oleracea var. botrytis) curds subjected to temperature stress and recovery involves regulation of the complexome, respiratory chain activity, organellar translation and ultrastructure. Biochim Biophys Acta. 2015 Jan 21. pii: S0005-2728(15)00016-X. doi: 10.1016/j.bbabio.2015.01.005.
Special application note:
Peptide used to elicit this antibody is not conserved in NADPH dependent anzymes, partially conserved across eukaryotic Idh subunits, Some conservation across bacterial which contain the NAD-dependent form of Idh (as opposed to the NADP-dependent form)
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 major light-harvesting antenna complex II (LHCII) in photosynthetic eukaryotes is located in the thylakoid membrane of the chloroplast. It is a heterotrimeric complex formed by up to 3 different individual subtypes of chlorophyll a/b-binding proteins: Lhcb1, Lhcb2, and Lhcb3. Lhcb2 is often coded by several nuclear genes and is found together with Lhcb1 within the mobile LHCII trimers involved in state1-state2 transition.A molecular characterisation of the LHCII proteins can be found in Caffarri et al. (2004) A Look within LHCII: Differential Analysis of the Lhcb1−3 Complexes Building the Major Trimeric Antenna Complex of Higher-Plant Photosynthesis. Biochemistry 43 (29): 9467–9476.
Product Type:
Antibody
Antibody Type:
Polyclonal
Format:
Lyophilized
Storage Temp:
Store lyophilized/reconstituted at -20 °C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
BSA-conjugated synthetic peptide derived from a highly conserved sequence of Lhcb2 proteins from angiosperms (monocots and dicots) and gymnosperms, including Arabidopsis thaliana Lhcb2.1 UniProt: Q9SHR7, TAIR: AT2G05100, Lhcb2.2 UniProt: Q9S7J7, TAIR:AT2G05070, Lhcb2.3 UniProt:Q9XF87, TAIR:AT3G27690
Applications:
Immunoprecipitation (IP), ImmunoGold (IG), Western blot (WB)
Immunoprecipitation has been done using Immunoprecipitation kit from Roche, Cat.No. 11 719 386 001.Protein is processed into mature form (Jansson 1999).
Application Details:
5 l of antibody solution (IP), 1: 100 (IG), 1: 500 - 1 : 5000 (WB)
Purity:
Immunogen affinity purified serum in PBS pH 7.4.
Reconstitution:
For reconstitution add 50 l of sterile water
Molecular Weight:
28.6 | 25 kDa for Arabidopsis thaliana
Not reactive in:
No confirmed exceptions from predicted reactivity are currently known
Selected references:
Singh, Muthamilarasan, Prasad (2022). SiHSFA2e regulated expression of SisHSP21.9 maintains chloroplast proteome integrity under high temperature stress. Cell Mol Life Sci. 2022;79(11):580. Published 2022 Nov 3. doi:10.1007/s00018-022-04611-10Cazzaniga et al. (2022). Engineering astaxanthin accumulation reduces photoinhibition and increases biomass productivity under high light in Chlamydomonas reinhardtii. Biotechnol Biofuels Bioprod. 2022 Jul 11;15(1):77. doi: 10.1186/s13068-022-02173-3. PMID: 35820961; PMCID: PMC9277849.Bru, Steen, Park, et al. (2022) The major trimeric antenna complexes serve as a site for qH-energy dissipation in plants. J Biol Chem. 2022;298(11):102519. doi:10.1016/j.jbc.2022.102521Ivanov et al. (2022) The decreased PG content of pgp1 inhibits PSI photochemistry and limits reaction center and light-harvesting polypeptide accumulation in response to cold acclimation. Planta 255, 36 (2022). https://doi.org/10.1007/s00425-022-03819-0Bychkov et al. (2022) The role of PAP4/FSD3 and PAP9/FSD2 in heat stress responses of chloroplast genes. Plant Sci. 2022 Sep;322:111359. doi: 10.1016/j.plantsci.2022.111359. Epub 2022 Jun 20. PMID: 35738478.
UniProt number:
Q9SHR7 , Q9S7J7 , Q9XF87 , Q9XF86
TAIR number:
AT2G05100
Research area:
LHC
Code:
Photo20
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