CD172a (SIRP alpha) Monoclonal Antibody (15-414), Super Bright™ 436, eBioscience™, Invitrogen™

Description

• Description: This 15-414 monoclonal antibody reacts with human CD172a, also known as signal regulatory protein alpha (SIRP alpha)
• This cell surface glycoprotein consists of three Ig-like extracellular domains and two cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs)
• The ITIM domains have been demonstrated to recruit and bind the Src homology 2 domain-containing phosphatases SHP-1 and SHP-2
• CD172a is expressed on monocytes, granulocytes, dendritic cells, and CD34+CD38- hematopoietic progenitor cells but not on T and B lymphocytes
• Moreover, neurons have also been shown to express CD172
• The integrin-associated protein CD47 is the extracellular ligand for CD172a
• Studies show that CD172a is involved in dendritic cell-mediated T cell activation, neutrophil migration, and phagocytosis
• Applications Reported: This 15-414 antibody has been reported for use in flow cytometric analysis
• Applications Tested: This 15-414 antibody has been pre-titrated and tested by flow cytometric analysis of normal human peripheral blood cells
• This can be used at 5 μL (0.5 μg) per test
• A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL
• Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test
• Super Bright 436 can be excited with the violet laser line (405 nm) and emits at 436 nm
• We recommend using a 450/50 bandpass filter, or equivalent
• SIRP alpha (CD172a, signal-regulatory protein alpha) is a receptor-type transmembrane glycoprotein expressed on cells of myeloid origin, including granulocytes, dendritic cells (DCs), macrophages, mast cells and hematopoietic stem cells
• SIRP alpha acts as a substrate for several activated tyrosine kinases, including EGFR, PDGFR, src and insulin receptor and is involved in the negative regulation of receptor tyrosine kinase-coupled signaling pathways
• The ligand binding of SIRP alpha to integrin-associated protein CD47 results in tyrosine kinase phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIMs) within the cytoplasmic region of SIRP alpha, which mediates the recruitment and activation of the tyrosine phosphatases SHP-1 and SHP-2
• Ligation of SIRP alpha with CD47 has been demonstrated in several regulatory processes, including the inhibition of host cell phagocytosis by macrophages and the bi-directional activation of T cells and DCs
• SIRP alpha has regulatory effects on cellular responses induced by serum, growth factors, insulin, oncogenes, growth hormones and cell adhesion, and plays a general role in different physiological and pathological processes
• Cancer cells highly express CD47, which activates SIRP alpha and inhibits macrophage-mediated destruction of cancerous cell growth.