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| | Met (L6E7) Mouse mAb Chemical Properties |
| | Met (L6E7) Mouse mAb Usage And Synthesis |
| Source | Mouse | | Reactivity | Human | | Background | Met, a high affinity tyrosine kinase receptor for hepatocyte growth factor is a disulfide-linked heterodimer made of 45 kDa α- and 145 kDa β-subunits. 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. These fundamental events are important for all of the biological functions involving Met kinase activity. The addition of a phosphate at cytoplasmic Tyr1003 is essential for Met protein ubiquitination and degradation. Phosphorylation at Tyr1234/1235 in the Met kinase domain is critical for kinase activation. Phosphorylation at Tyr1349 in the Met cytoplasmic domain provides a direct binding site for Gab1. Research studies have shown that altered Met levels and/or tyrosine kinase activities are found in several types of tumors, including renal, colon, and breast. Thus, investigators have concluded that Met is an attractive potential cancer therapeutic and diagnostic target. | | References | [1] Cooper, C.S. et al. (1984) Nature 311, 29-33.
[2] Bottaro, D.P. et al. (1991) Science 251, 802-4.
[3] Bardelli, A. et al. (1997) Oncogene 15, 3103-11.
[4] Taher, T.E. et al. (2002) J Immunol 169, 3793-800.
[5] Schaeper, U. et al. (2000) J Cell Biol 149, 1419-32.
[6] Eder, J.P. et al. (2009) Clin Cancer Res 15, 2207-14.
[7] Sattler, M. and Salgia, R. (2009) Update Cancer Ther 3, 109-118. |
| | Met (L6E7) Mouse mAb Preparation Products And Raw materials |
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