Invitrogen™ CD172a (SIRP alpha) Monoclonal Antibody (P84), PE, eBioscience™, Invitrogen™

Beschreibung

Description: This P84 monoclonal antibody reacts with mouse CD172a, also known as signal regulatory protein a (SIRPa). 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, macrophages, dendritic cells, but not on T and B lymphocytes. Moreover, neurons and other tissues of the central nervous system have also been shown to express CD172a. 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. This monoclonal antibody has been reported to have neutralizing activity. Applications Reported: This P84 antibody has been reported for use in flow cytometric analysis. Applications Tested: This P84 antibody has been tested by flow cytometric analysis of mouse bone marrow cells. This can be used at less than or equal to 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. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest.

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.