mouse monoclonal IgG1; SIRP-α/β Antibody (A-1) is an IgG1 κ mouse monoclonal SIRP- alpha / beta antibody (also designated SIRP alpha/beta antibody or SIRPa/b antibody) that detects the SIRP- alpha / beta protein of human origin by WB, IP, IF, IHC(P) and ELISA. SIRP-α/β Antibody (A-1) is available as both the non-conjugated anti-SIRP- alpha / beta antibody form, as well as multiple conjugated forms of anti-SIRP- alpha / beta antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. SIRPs (signal-regulatory proteins) are a family of transmembrane glycoproteins that were identified by their association with the Src homology 2 domain-containing protein-tyrosine phosphatase SHP-2 in response to insulin. The SIRP family negatively regulates the PI 3-kinase pathway, which may diminish EGFR-mediated motility and survival phenotypes that contribute to transformation of certain cell types. SIRP-α1 is a transmembrane protein which contains an extracellular portion with three immunoglobulin-like structures and a cytoplasmic region with four potential tyrosine phosphorylation sites. SIRP-α (also known as SIRP-α1, SIRP-α2 or SIRP-α3) is a substrate for activated receptor tyrosine kinases. In its tyrosine phosphorylated form, SIRP-α binds to SH-PTP2 through SH2 interactions and acts as an SH-PTP2 substrate. SIRP-α has been shown to have negative regulatory effects on cellular responses induced by growth factors, oncogenes and insulin. SIRP-β1 shares extensive sequence homology with SIRP-α in its extracellular portion but lacks the cytoplasmic portion. SIRP-γ, originally designated SIRP-β2 (SIRP-B2, CD172g) has unique characteristics from both the α and β versions. SIRP-γ is expressed on the majority of T cells and a proportion of B cells. CD47 associates with SIRP-γ, and this interaction signals unidirectionally only.