GRADE & PURITYAnimal Free?Animal-free — produced without animal-derived components to reduce contamination risk. Use in biomanufacturing and culture avoiding animal-origin material.Carrier Free?Carrier-free — supplied without added carrier protein/stabilizer. Use when carriers (e.g. BSA) would interfere with conjugation or sensitive assays.Bioactive?Bioactive grade — verified to retain biological activity in functional assays. Use when the molecule must be functionally active, not just pure.ActiBioPure™?ActiBioPure™ — Aladdin's premier line for bioactive and recombinant products. Use when both high purity and preserved biological activity are required.Azide Free?Azide-free — without sodium azide preservative. Use in conjugations, cell work, or assays where azide is toxic or inhibitory.His Tag?His tag grade — recombinant protein bearing a His tag for affinity purification/detection. Use to purify, immobilize, or detect the tagged protein.≥95%(SDS-PAGE)
Expression System
HEK293
Accession #
P08581
Protein Tag
C-His
Expression system
HEK293
Endotoxin Concentration
<1.0 EU/μg
Bioactivity
Immobilized Recombinant Human HGFR/c-MET Protein (rp169642) at 1.0 μg/mL can bind Recombinant human HGF protein (rp175908) with the ED50 is 97.73 ng/mL.
Animal Free,Carrier Free,Bioactive,ActiBioPure™,Azide Free,His-Tag,≥95%(SDS-PAGE) ActiBioPure™,Animal Free,Azide Free,Bioactive,Carrier Free,His Tag for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining Description: 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. 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. 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. The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization. Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules. HGF stimulation induces HGF R down-regulation via internalization and proteasome-dependent degradation. 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. Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects. Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion. 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. Genetic polymorphisms, chromosomal translocation, over-expression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers. Within the ECD, human HGF R shares 86%-88% aa sequence identity with canine, mouse, and rat HGF R.
Specifications
Product Name
Recombinant Human HGFR/c-MET Protein
Synonyms
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
Grade
ActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, His Tag
Immobilized Recombinant Human HGFR/c-MET Protein (rp169642) at 1.0 μg/mL can bind Recombinant human HGF protein (rp175908) with the ED50 is 97.73 ng/mL.
36.0-50.0 & 72.0-92.0, under reducing condition; 110.2-155.6 kDa, under non-reducing condition
Molecule Type
Protein
Storage and Shipping
Shape
Lyophilized
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Storage
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20°C stable up to 1 year. Avoid freeze/thaw cycle.
Images
Recombinant Human HGFR/c-MET Protein (rp169642) - Protein Bioactivity Immobilized Recombinant Human HGFR/c-MET Protein (rp169642) at 1.0 μg/mL can bind Recombinant human HGF protein (rp175908) with the ED₅₀ is 97.73 ng/mL.
Recombinant Human HGFR/c-MET Protein (rp169642) - SDS-PAGE 3 μg/lane of Recombinant Human HGFR/c-MET Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 36.0-50.0 & 72.0-92.0 kDa under reducing conditions and 110.2-155.6 kDa under non-reducing conditions. Heterodimer made of an alpha chain and a beta chain which are disulfide linked (Uniprot: P08581).
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
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