Recombinant Human HGFR/c-MET Fc Chimera His-tag Protein Summary
Product Specifications
Kd <0.5 nM.
HGF R alpha (Glu25-Arg307) Accession # P08581 |
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HGF R beta (Ser308-Thr932) Accession # P08581 |
HIEGRMD | Human IgG1 (Pro100-Lys330) |
6 His tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
358-MT (with carrier)
358-MT/CF (carrier free)
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
358-MT
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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358-MT/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: HGFR/c-MET
HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta -propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). Proteolysis and alternate splicing generate additional forms of human HGF R which either lack of the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the alpha and beta chains (5-7). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 8). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (9, 10). HGF stimulation induces HGF R down-regulation via internalization and proteasome-dependent degradation (11). In the absence of ligand, HGF R forms noncovalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, Integrin alpha 6/ beta 4, Plexins B1, 2, 3, and MSP R/Ron (12-19). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (12-19). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (12, 16, 17). Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells (20). Genetic polymorphisms, chromosomal translocation, over-expression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86%-88% aa sequence identity with canine, mouse, and rat HGF R.
- Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.
- Corso, S. et al. (2005) Trends Mol. Med. 11:284.
- Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. 100:12039.
- Park, M. et al. (1987) Proc. Natl. Acad. Sci. 84:6379.
- Crepaldi, T. et al. (1994) J. Biol. Chem. 269:1750.
- Prat, M. et al. (1991) Mol. Cell. Biol. 12:5954.
- Rodrigues, G.A. et al. (1991) Mol. Cell. Biol. 11:2962.
- Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
- Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
- Ponzetto, C. et al. (1994) Cell 77:261.
- Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
- Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
- Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
- Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
- Wang, X. et al. (2002) Mol. Cell 9:411.
- Trusolino, L. et al. (2001) Cell 107:643.
- Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
- Conrotto, P. et al. (2004) Oncogene 23:5131.
- Follenzi, A. et al. (2000) Oncogene 19:3041.
- Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223.
Citations for Recombinant Human HGFR/c-MET Fc Chimera His-tag Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 6
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Cellular signaling and gene expression profiles evoked by a bivalent macrocyclic peptide that serves as an artificial MET receptor agonist
Authors: W Miao, K Sakai, N Ozawa, T Nishiuchi, Y Suzuki, K Ito, T Morioka, M Umitsu, J Takagi, H Suga, K Matsumoto
Sci Rep, 2018-11-07;8(1):16492.
Applications: Bioassay -
Tumor and Plasma Met Levels in Non-Metastatic Prostate Cancer
Authors: Deborah R Kaye
PLoS ONE, 2016-06-14;11(6):e0157130.
Species: Human
Sample Types: Whole Tissue
Applications: ELISA (Standard) -
A Novel Bispecific Antibody Targeting EGFR and cMet that is Effective Against EGFR Inhibitor- Resistant Lung Tumors
Cancer Res, 2016-05-23;0(0):.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay -
LY2875358, a neutralizing and internalizing anti-MET bivalent antibody, inhibits HGF-dependent and HGF-independent MET activation and tumor growth.
Authors: Liu L, Zeng W, Wortinger M, Yan S, Cornwell P, Peek V, Stephens J, Tetreault J, Xia J, Manro J, Credille K, Ballard D, Brown-Augsburger P, Wacheck V, Chow C, Huang L, Wang Y, Denning I, Davies J, Tang Y, Vaillancourt P, Lu J
Clin Cancer Res, 2014-09-17;20(23):6059-70.
Species: Mouse
Sample Types: In Vivo
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A pharmacodynamic/pharmacokinetic study of ficlatuzumab in patients with advanced solid tumors and liver metastases.
Authors: Tabernero J, Elez M, Herranz M, Rico I, Prudkin L, Andreu J, Mateos J, Carreras M, Han M, Gifford J, Credi M, Yin W, Agarwal S, Komarnitsky P, Baselga J
Clin Cancer Res, 2014-03-14;20(10):2793-804.
Species: Human
Sample Types: Serum
Applications: ELISA (Standard) -
Bi-specific Aptamers Mediating Tumor Cell Lysis.
Authors: Boltz A, Piater B, Toleikis L, Guenther R, Kolmar H, Hock B
J. Biol. Chem., 2011-04-29;286(24):21896-905.
Species: Human
Sample Types: DNA
Applications: Bioassay
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