Recombinant Human HGFR/c-MET Fc Chimera His-tag Protein

Carrier Free

Catalog # Availability Size / Price Qty
358-MT-100/CF

With Carrier

Catalog # Availability Size / Price Qty
358-MT-100
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Citations (6)
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Recombinant Human HGFR/c-MET Fc Chimera His-tag Protein Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind rhHGF in a functional ELISA with an estimated K d <0.5 nM.
Source
Mouse myeloma cell line, NS0-derived human HGF R/c-MET protein
HGF R alpha (Glu25-Arg307) Accession # P08581 HGF R beta (Ser308-Thr932) Accession # P08581 HIEGRMD Human IgG 1 (Pro100-Lys330) 6 His tag N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Glu25 & Ser308
Structure / Form
Tetramer containing two disulfide-linked proteolytically cleaved alpha and beta subunits
Predicted Molecular Mass
32.5 kDa (alpha chain), 96.7 kDa (beta chain)
SDS-PAGE
43-50 kDa (alpha chain) and 120-125 kDa (beta chain), reducing conditions

Product Datasheets

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358-MT (with carrier)

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358-MT/CF (carrier free)

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.
    12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.

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.
    12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Reconstitution Calculator

Reconstitution Calculator

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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.

References
  1. Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.
  2. Corso, S. et al. (2005) Trends Mol. Med. 11:284.
  3. Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. 100:12039.
  4. Park, M. et al. (1987) Proc. Natl. Acad. Sci. 84:6379.
  5. Crepaldi, T. et al. (1994) J. Biol. Chem. 269:1750.
  6. Prat, M. et al. (1991) Mol. Cell. Biol. 12:5954.
  7. Rodrigues, G.A. et al. (1991) Mol. Cell. Biol. 11:2962.
  8. Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
  9. Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
  10. Ponzetto, C. et al. (1994) Cell 77:261.
  11. Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
  12. Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
  13. Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
  14. Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
  15. Wang, X. et al. (2002) Mol. Cell 9:411.
  16. Trusolino, L. et al. (2001) Cell 107:643.
  17. Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
  18. Conrotto, P. et al. (2004) Oncogene 23:5131.
  19. Follenzi, A. et al. (2000) Oncogene 19:3041.
  20. Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223.
Long Name
Hepatocyte Growth Factor Receptor
Entrez Gene IDs
4233 (Human); 17295 (Mouse)
Alternate Names
AUTS9; cMET; c-MET; EC 2.7.10; EC 2.7.10.1; hepatocyte growth factor receptor; HGF R; HGF receptor; HGF/SF receptor; HGFR; Met (c-Met); met proto-oncogene (hepatocyte growth factor receptor); met proto-oncogene tyrosine kinase; MET; oncogene MET; Proto-oncogene c-Met; RCCP2; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met

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.

6 Citations: Showing 1 - 6
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  1. 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
  2. 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)
  3. 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
  4. 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
  5. 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)
  6. 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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Recombinant Human HGFR/c-MET Fc Chimera His-tag Protein
By Anonymous on 12/06/2020
Application: Immunoassay Standard