Phospho-Syk (Tyr525/526) Antibody

INQUIRY

CAT. NO.: AMA-0326

Target Information
UniProt ID	P43405

Product Details
Size	100 µL
Reactivity	Human
Storage	Store at -20°C. Do not aliquot the antibody.
Purification	Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr525/526 of human Syk. Antibodies are purified by protein A and peptide affinity chromatography.

Usage
Application	WB
Product Usage Information Dilution	Western Blotting (1:1000)
MW (Target)	72 kDa

Background
Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl Tyr352 of Syk is involved in the association of PLCγ1 Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function.

Background

Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl Tyr352 of Syk is involved in the association of PLCγ1 Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function.

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