Anti-SLP65 / BLNK Polyclonal Antibody

SLP65 / BLNK (SH2 domain-containing leukocyte-specific phosphoprotein of 65 kDa; B cell linker protein), also known as BASH, is an adaptor protein that plays key role in B cell activation initiated by cross-linking the B cell receptor (BCR). Phosphorylated by Syk tyrosine kinase, SLP65 serves as a scaffold for Btk tyrosine kinase, Vav1 guanine nucleotide exchange factor, phospholipase C gamma2, as well as Grb2 and Nck adaptor proteins; thus represents a central linker protein that bridges the BCR-associated kinases with a multitude of signaling pathways.

Subcellular location:	Cytoplasm, Cell membrane
Post transnational modification:	Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+) and MAPK signaling pathways (By similarity). Phosphorylation of Tyr-96 is required for the binding of BTK.
Tissue Specificity:	Expressed in the spleen and weakly in thymus, no expression was seen in liver, testis, or brain. Expressed in B-cell lines representing different developmental stages from the pre-B to the plasma cell stage, but not in a T-cell or a fibroblast cell line.
BioGrid:	201236. 5 interactions.

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