Recombinant human Met (c-Met) (mutated L1195V) protein (Active)
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Recombinant human Met (c-Met) (mutated L1195V) protein (Active) is a Human Full Length protein, in the 956 to 1390 aa range, expressed in Insect cells, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
Hepatocyte growth factor receptor, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, Tyrosine-protein kinase Met, SF receptor, MET
- FuncS
Supplier Data
Functional Studies - Recombinant human Met (c-Met) (mutated L1195V) protein (Active) (AB268772)
The specific activity of ab268772 was 40 nmol/min/mg in a peptide kinase assay using Poly(4 : 1 Glu, Tyr) as substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Met (c-Met) (mutated L1195V) protein (Active) (AB268772)
SDS-PAGE analysis of ab268772.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (By similarity). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity).. (Microbial infection) Acts as a receptor for Listeria monocytogenes internalin InlB, mediating entry of the pathogen into cells.
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family.
Post-translational modifications
Autophosphorylated in response to ligand binding on Tyr-1234 and Tyr-1235 in the kinase domain leading to further phosphorylation of Tyr-1349 and Tyr-1356 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1349 and Tyr-1365. Dephosphorylated by PTPN1 and PTPN2.. Ubiquitinated. Ubiquitination by CBL regulates MET endocytosis, resulting in decreasing plasma membrane receptor abundance, and in endosomal degradation and/or recycling of internalized receptors.. O-mannosylation of IPT/TIG domains by TMEM260 is required for protein maturation (PubMed:37186866). O-mannosylated residues are composed of single mannose glycans that are not elongated or modified (PubMed:37186866).. (Microbial infection) Tyrosine phosphorylation is stimulated by L.monocytogenes InlB. Tyrosine phosphorylation is maximal 10-20 minutes after treatment with InlB and disappears by 60 minutes. The phosphorylated residues were not identified.
Product protocols
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Target data
Product promise
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