Phospho-BLNK (Tyr96) Antibody detects endogenous levels of BLNK only when phosphorylated at tyrosine 96.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Tyr96 of human BLNK. Antibodies are purified by protein A and peptide affinity chromatography.
Background
BLNK (B cell linker protein), also known as SLP-65 or BASH, is an adaptor molecule that plays key roles in B cell activation and B cell antigen receptor (BCR) engagement. BLNK acts on the interface between BCR-associated Syk and the downstream signaling cascades (1,2). BLNK has multiple SH2 binding motifs (YXXP) at its amino-terminus and a SH2 domain at its carboxy-terminus. After BCR ligation, BLNK is phosphorylated by Syk at multiple YXXP motifs including Tyr72, Tyr84, Tyr96 and Tyr178 (1). These phosphorylated motifs provide docking sites for signaling molecules such as Btk, PLCgamma and Vav. These signaling molecules bind to BLNK through their SH2 domains and together activate downstream signaling pathways (3,4). Through its SH2 domain, BLNK can also interact with tyrosine-phosphorylated targets such as HPK1 to recruit it to the BCR complex for signaling (5).