Phospho-Syk (Ser323) and Phospho-Syk (Tyr525/526) Antibodies detect transfected, Tyr323 and Tyr 525/526 phosphorylated human Syk. Syk Antibody and Phospho-Zap-70 (Tyr319)/Syk (Tyr352) Antibodies detect endogenous levels of total human Syk and Tyr352 phosphorylated Syk, respectively. Each phospho-Syk antibody recognizes only the specific phosphorylated form of Syk. The control Syk Antibody recognizes both nonphosphorylated and phosphorylated forms of Syk. Phospho-Zap-70 (Tyr319)/Syk (Tyr352) Antibody cross-reacts with the phosphorylated form of Zap-70. All other antibodies in the kit do not cross-react with phosphorylated or nonphosphorylated forms of other related family members.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Tyr323, Tyr352 or Tyr525/526 of human Syk. The control Syk Antibody is produced by immunizing rabbits with a synthetic nonphosphopeptide corresponding to the carboxy terminal sequence of human Syk. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Description
Phospho-Syk Sampler Kit provides an economical means to evaluate the activation status of Syk, including the phosphorylation of Tyr323, Tyr352 and Tyr525/526. The control Syk Antibody is also included. The kit contains enough primary and secondary antibodies for four Western blot experiments.
Background
Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells, and Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation of Tyr323 provides a direct binding site to the TKB domain of Cbl (6,7). Tyrosine 352 of Syk is involved in the association of PLC-γ1 (8). Tyrosines 525 and 526 are located in the activation loop of the Syk kinase domain, and phosphorylation of Tyr525/526 of human Syk (equivalent to the Tyr519/520 of mouse Syk) is essential for Syk function (9).