Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF
Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF Summary
Product Specifications
KD <0.2 nM.
Mouse HGF R (Met1 - Asn929) Accession # P16056 |
DIEGRMD | Human IgG1 (Pro100 - Lys330) |
6-His tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
527-ME
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.
527-ME
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
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.
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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). An alternately spliced form of mouse HGF R lacks a cytoplasmic juxtamembrane region important for regulation of signal transduction (5, 6). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 7). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (8, 9). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (10). 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 (11 - 18). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (11 - 18). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (11, 15, 16). 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 (19). Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, mouse HGF R shares 87%, 87%, and 94% amino acid sequence identity with canine, human, and rat HGF R, respectively.
- 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.
- Chan, A.M. et al. (1988) Oncogene 2:593.
- Lee, C.-C. and K.M. Yamada (1994) J. Biol. Chem. 269:19457.
- Lee, C.-C., et al. (1995) J. Biol. Chem. 270:507.
- 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 Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF
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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Machine Learning-Guided Prediction of Antigen-Reactive In Silico Clonotypes Based on Changes in Clonal Abundance through Bio-Panning
Authors: DK Yoo, SR Lee, Y Jung, H Han, HK Lee, J Han, S Kim, J Chae, T Ryu, J Chung
Biomolecules, 2020-03-08;10(3):.
Species: Gallus domesticus (Chicken)
Sample Types: In Vivo
Applications: In Vivo -
RhoA/phosphatidylinositol 3-kinase/protein kinase B/mitogen-activated protein kinase signaling after growth arrest-specific protein 6/mer receptor tyrosine kinase engagement promotes epithelial cell growth and wound repair via upregulation of hepatocyte growth factor in macrophages.
Authors: Lee Y, Park H, Woo S, Park E, Kang J
J Pharmacol Exp Ther, 2014-06-17;350(3):563-77.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
A role for calcium-calmodulin in regulating nitric oxide production during skeletal muscle satellite cell activation.
Authors: Tatsumi R, Wuollet AL, Tabata K, Nishimura S, Tabata S, Mizunoya W, Ikeuchi Y, Allen RE
Am. J. Physiol., Cell Physiol., 2009-01-21;296(4):C922-9.
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay
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