This gene encodes a subunit of the transcription factor complex nuclear factor-kappa-B (NFkB). The NFkB complex is expressed in numerous cell types and functions as a central activator of genes involved in inflammation and immune function. The protein encoded by this gene can function as both a transcriptional activator or repressor depending on its dimerization partner. The p100 full-length protein is co-translationally processed into a p52 active form. Chromosomal rearrangements and translocations of this locus have been observed in B cell lymphomas, some of which may result in the formation of fusion proteins. There is a pseudogene for this gene on chromosome 18. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2013]
Product Type:
Antibodies Primary
Antibody Type:
monoclonal
Storage Temp:
4°C -20°C for long term storage
Immunogen:
Purified recombinant fragment of human NFKB2 (AA: 712-900) expressed in E. Coli.
The protein encoded by this gene is a lymphocyte-specific member of the tumor necrosis factor (TNF) receptor superfamily. It interacts with calcium-modulator and cyclophilin ligand (CAML). The protein induces activation of the transcription factors NFAT, AP1, and NF-kappa-B and plays a crucial role in humoral immunity by interacting with a TNF ligand. This gene is located within the Smith-Magenis syndrome region on chromosome 17. [provided by RefSeq, Jul 2008]
Product Type:
Antibodies Primary
Storage Temp:
4°C -20°C for long term storage
Immunogen:
Purified recombinant fragment of human CD267 (AA: extra(1-165)) expressed in E. Coli.
Prohibitin is an evolutionarily conserved gene that is ubiquitously expressed. It is thought to be a negative regulator of cell proliferation and may be a tumor suppressor. Mutations in PHB have been linked to sporadic breast cancer. Prohibitin is expressed as two transcripts with varying lengths of 3' untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, suggesting that this longer 3' untranslated region may function as a trans-acting regulatory RNA.
Product Type:
Antibodies Primary
Antibody Type:
monoclonal
Storage Temp:
4°C -20°C for long term storage
Host Animal:
mouse
Immunogen:
Purified recombinant fragment of human PHB expressed in E. Coli.
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
CD45RA is a high molecular weight isoform of a receptor-type protein tyrosine phosphatase, CD45 glycoprotein. CD45 is crucial in lymphocyte development and antigen signaling, serving as an important regulator of Src-family kinases, promotes cell survival by modulating integrin-mediated signal transduction pathway and is also involved in DNA fragmentation during apoptosis. CD45 isoforms differ in their extracellular domains, whereas they share identical transmembrane and cytoplasmic domains. These isoforms differ in their ability to translocate into the glycosphingolipid-enriched membrane domains and their expression depends on cell type and physiological state of the cell. CD45RA is expressed e.g. on naïve T cells and normal plasma cells.
Product Type:
Antibodies Primary
Antibody Type:
monoclonal
Storage Temp:
Store at 2-8°C. Protect from prolonged exposure to light. Do not freeze.
Immunogen:
Human thymocytes and T lymphocytes.
Applications:
FC
Additional Info:
The antibody MEM-56 reacts with an extracellular epitope of CD45RA, a 205-220 kDa single chain type I glycoprotein, variant of CD45 (CD45RA isoform). CD45RA is expressed on most of B lymphocytes, resting and native T lymphocytes, medullar thymocytes and monocytes.
Clone number:
MEM-56
Antibody Isotype:
IgG2b
Application Details:
Flow cytometry: The reagent is designed for analysis of human blood cells using 4 ?l reagent / 100 ?l of whole blood or 106 cells in a suspension. The content of a vial (0.4 ml) is sufficient for 100 tests.
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 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.
Antibody Isotype:
IgG1
Monosan Range:
MONOSAN
Clone:
T2.5
Concentration:
100 ug/ ml
Storage buffer:
PBS with 0.1% BSA and 0.02% sodium azide
Storage:
2-8°C
References 1:
Meng; G et al. J Clin Invest 2004; 113: 1473
References 2:
Roura-Mir, C et al J Immunol 2005, 175: 1758
References 3:
Leemans; J et al. J Clin Invest 2005 115: 2894
References 4:
Spiller S et al. JEM 2008; 205: 1747
References 5:
Sutmuller R et al. J Clin Invest 2006; 116:485
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