|Phospho-Gab1 (Tyr307) Antibody 3234||20 µl||
|Gab1 Antibody 3232||20 µl||
||H M R Mk||110||Rabbit|
|Phospho-Met (Tyr1003) (13D11) Rabbit mAb 3135||20 µl||
||H M R||145||Rabbit IgG|
|Phospho-Met (Tyr1234/1235) (D26) XP® Rabbit mAb 3077||20 µl||
||H M R||145||Rabbit|
|Phospho-Met (Tyr1349) (130H2) Rabbit mAb 3133||20 µl||
||H M R||145||Rabbit|
|Met (D1C2) XP® Rabbit mAb 8198||20 µl||
||H||140, 170||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Monoclonal antibodies are produced by immunizing animals with synthetic phosphopeptides or peptides corresponding to residues surrounding: Tyr1003, Tyr1234/1235, Tyr1349, or near the carboxy terminus of human Met protein. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide or peptide corresponding to residues surrounding Tyr472 and Tyr307 of human Gab1. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Met, a high affinity tyrosine kinase receptor for hepatocyte growth factor (HGF, also known as scatter factor), is a disulfide-linked heterodimer made of 45 kDa α- and 145 kDa β-subunits (1,2). The α-subunit and the amino-terminal region of the β-subunit form the extracellular domain. The remainder of the β-chain spans the plasma membrane and contains a cytoplasmic region with tyrosine kinase activity. Interaction of Met with HGF results in autophosphorylation at multiple tyrosines, which recruit several downstream signaling components, including Gab1, c-Cbl and PI3 kinase (3). These fundamental events are important for all of the biological functions involving Met kinase activity. Addition of a phosphate at cytoplasmic Tyr1003 is essential for ubiquitination and Met protein degradation (4). Phosphorylation of Tyr1234/1235 in the Met kinase domain is critical to kinase activation. Phosphorylation of Tyr1349 in the Met cytoplasmic domain provides a direct binding site for Gab1 (5). Altered Met levels and/or tyrosine kinase activities are found in several types of tumors, including renal, colon and breast cancers. Thus, Met is an attractive cancer therapeutic and diagnostic target (6).
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