Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein, CF
Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein, CF Summary
Product Specifications
| Cynomolgus HGFR/c-MET (Glu25-Thr932) Accession # EHH52447.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
11267-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.
11267-ME
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in 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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Scientific Data
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Measured by its binding ability in a functional ELISA. When Recombinant Human HGF (NS0-expressed) Protein (11352-HG) is immobilized at 0.250 μg/mL (100 μL/well), Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein (Catalog # 11267-ME) binds with an ED50 of 2.50-25.0 ng/mL.
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2 μg/lane of Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein (Catalog # 11267-ME) was resolved with SDS-PAGE and visualized by Coomassie® Blue staining, showing bands at 135-150 kDa, 40-45 kDa, and 103-115 kDa under reducing (R) conditions and a single band at 270-310 kDa under non-reducing (NR) conditions.
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. Based on the high homology (98%) between cynomolgus and human HGF R, cynomolgus HGF R is predicted to be 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 alternative 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, 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 down-regulation 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, 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.
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