Anti-phospho-c-Met (pTyr¹²³⁰/pTyr¹²³⁴/pTyr¹²³⁵) antibody produced in rabbit

Detection of phospho-c-Met by immunoblotting may be performed by using a working concentration of 0.11.0 μg/mL in 293T kidney cells, SP-1 mouse myeloma cells stimulated with HGF and A431 cells stimulated with EGF.

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MET, a gene for receptor tyrosine kinase, was first isolated in human osteosarcoma-derived cell line. Hepatocyte growth factor (HGF) has been identified as the natural ligand for the c-Met receptor protein. HGF-induced c-Met activation is tightly regulated in the cells. Activation of the c-Met receptor results in binding and/or phosphorylation of many intracellular signaling proteins including multiple adaptor proteins (e.g., Grb2, Shc, Cbl, Crk, cortactin, paxillin, and GAB1) and a variety of other signal transducers (e.g., PI 3-kinase, FAK, Src, ERK1, JNK1, PLCa, and STAT3). HGF/Met signalling is actively responsible stimulating tumor angiogenesis, tumor growth, hypoxia and metastasis. Met overexpression through persistent ligand stimulation has been reported in many epithelial and mesenchymal cancers. Overexpression of Met enables metastasis in lung cancers, mutations in MET gene sequence have been reported in papillary renal cell carcinoma, lung cancers, ovarian, prostate, cervical, gastric and head and neck cancers. Anti-phospho-c-Met recognises human and mouse c-Met phosphorylated on Tyr1230, Tyr1234 and Try1235. Cross reaction with rat is expected due to 100% homology.

synthetic phosphopeptide derived from the region of c-Met that contains tyrosines 1230, 1234 and 1235.

Solution in Dulbecco′s phosphate buffered saline (without Mg²⁺ and Ca²⁺), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG and protease free) and 0.05% sodium azide.