BAFF-R (CT) Blocking Peptide
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Antibody DetailsProduct DetailsReactive Species Human Product Concentration 0.2 mg/ml Amino Acid Location This peptide sequence is located at amino acids 169 to 183 of Human BAFF-R protein. Formulation This peptide is formulated in PBS pH 7.2 (0.01 M Sodium Phosphate, 0.13 M NaCl) containing 0.1% bovine serum albumin and 0.02% sodium azide. Storage and Handling Store this peptide in working aliquots at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Next Day Ambient Amino Acid Sequence 15 amino acids near the carboxy terminus of human BAFF Receptor. Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionBackground BAFF receptor (BAFFR) is a type III transmembrane protein and member of the TNF receptor (TNFR) super family. It is highly expressed in spleen, lymph node, B-cells and peripheral blood leukocytes. BAFFR plays a role in nearly all stages of differentiation of B-cells from development to the maintenance of long-lived bone marrow plasma cells. BAFFR signals by activation of the NF-kappaB signaling pathway. Overexpression of the BAFFR ligand, BAFF, in mice leads to autoimmune characteristics similar to systemic lupus erythematosus (SLE) and Sjogren’s syndrome. Furthermore, high levels of BAFF have been detected in the serum of humans with SLE, rheumatoid arthritis, Sjogren’s syndrome and systemic sclerosis. Inhibition of BAFFR signaling with BAFFR-Ig has been successful in treating SLE and rheumatoid arthritis in mouse models. In addition misexpression of BAFFR brought about by retroviral integration has lead to leukemia in some strains of mice. This makes BAFFR an obvious candidate for further therapeutic investigation. Recombinant human BAFFR has a molecular weight of 7.7 kDa and contains 76 amino acid residues corresponding to the extracellular portion of the full native BAFFR. References & Citations1. Tschopp J, Martinon F, and Burns K. NALPs: a novel protein family involved in inflammation. Nat. Rev. Mol. Cell Biol. 2003; 4:95-104.
2. Bruey JM, Bruey-Sedano N, Newman R, et al. PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-κB and caspase-1 activation in macrophages. J. Biol. Chem. 2004; 279:51897-907.
3. Agostini L, Martinon F, Burns K, et al. NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 2004; 20:319-25.
4. Martinon F and Tschopp J. NLRs join TLRs as innate sensors of pathogens. TRENDS Imm. 2005; 26:447-54. |
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