#65060 Phospho-BLNK (Tyr84) Antibody
|Phospho-BLNK (Tyr84) Antibody recognizes endogenous levels of BLNK protein only when phosphorylated at Tyr84. This antibody cross-reacts with phospho-Her2.|
|Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr84 of human BLNK protein. Antibodies are purified by protein A and peptide affinity chromatography.|
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Western blot analysis of extracts from Ramos cells, untreated (-) or treated with anti-human IgM (12μg/ml, 10 min), using Phospho-BLNK (Tyr84) Antibody (upper) or BLNK (D3P2H) XP® Rabbit mAb #36438 (lower).
Immunoprecipitation of Phospho-BLNK (Tyr84) from Ramos cell extracts treated with anti-human IgM (12 μg/ml, 5 min). Lane 1 is 10% input, lane 2 is Normal Rabbit IgG #2729, and lane 3 is Phospho-BLNK (Tyr84) Antibody. Western blot analysis was performed using Phospho-BLNK (Tyr84) Antibody.
B cell linker protein (BLNK), 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 at the interface between BCR-associated Syk and downstream signaling cascades (1,2). BLNK has multiple SH2 binding motifs (YXXP) at its amino terminus and an 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, PLCγ, 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, thereby recruiting them to the BCR complex for signaling (5).
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