Syk is a member of the family of non-receptor type protein-tyrosine kinases and plays a crucial role in lymphocyte signaling and development. Syk is expressed in all hematopoietic cells and contributes to the signal transduction process by binding to a tyrosine-based activation motif (ITAM) of immune receptors, including Igalpha, TCRzeta, CD3epsilon, FcepsilonRIbeta, and FceRIgamma. Upon receptor activation, Syk binds to phosphorylated ITAMs via its two N-terminal SH2 domains, thereby activating Syk and causing tyrosines in Syk to undergo auto-phosphorylation or phosphorylation. These phosphorylated sites can act as binding sites for other signaling molecules or help to regulate enzymatic activity. For example, in mast cells, Syk can activate downstream targets such as phospholipase Cgamma1 and VAV. Studies in Syk-/- mast cells identified defects in both the ERK-MAP and JNK-MAP kinase pathways.
Clone M373 was generated from a sequence corresponding to amino acids in the central region of human Syk. This sequence has high homology to mouse and rat Syk.
Target:
Syk (Central region)
Application Dilute:
WB(1:300-5000)
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