CD172g polyclonal antibody

SIRPs (signal-regulatory proteins) are a family of transmembrane glycoproteins that were identified by their association with the Src homology 2 domain_x0002_containing protein-tyrosine phosphatase SHP-2 in response to Insulin. The SIRP family negatively regulates the PI 3-K pathway, which may diminish EGFR-mediated motility and survival phenotypes that contribute to transforma_x0002_tion of certain cell types. SIRP-α1 is a transmembrane protein which contains an extracellular portion with three immunoglobulin-like structures and a cyto_x0002_plasmic region with four potential tyrosine phosphorylation sites. SIRP-α1 is a substrate for activated receptor tyrosine kinases. In its tyrosine phosphoryl_x0002_ated form, SIRP-α1 binds to SH-PTP2 through SH2 interactions and acts as an SH-PTP2 substrate. SIRP-α1 has been shown to have negative regulatory effects on cellular responses induced by growth factors, oncogenes and insu_x0002_lin. SIRP-b1 shares extensive sequence homology with SIRP-α1 in its extra_x0002_cellular portion but lacks the cytoplasmic portion. SIRP-g, originally designated SIRP-b2 (SIRP-B2, CD172g) has unique characteristics from both the α and b versions. SIRP-g is expressed on the majority of T cells and a proportion of B cells. CD47 associates with SIRP-g, and this interaction signals unidirec_x0002_tionally only.

Signal-regulatory protein gamma; SIRP-gamma; CD172 antigen-like family member B; Signal-regulatory protein beta-2; SIRP-b2; SIRP-beta-2; CD172g; SIRPG; SIRPB2

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .