Recombinant Human HGF R (C-Fc)

Recombinant Human HGF R (C-Fc)

Size1:10μg price1:$66
Size2:50μg price2:$186
Size3:500μg price3:$930
SKU: PHH0790 Category: Target Proteins Tags: ,

Datasheet

Name

Recombinant Human HGF R (C-Fc)

Purity

Greater than 95% as determined by reducing SDS-PAGE

Endotoxin level

<1 EU/µg as determined by LAL test.

Construction

Recombinant Human Hepatocyte Growth Factor Receptor is produced by our Mammalian expression system and the target gene encoding Glu25-Thr932 is expressed with a human IgG1 Fc tag at the C-terminus.

Accession #

P08581

Host

Human Cells

Species

Human

Predicted Molecular Mass

128.4 KDa

Buffer

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Form

Lyophilized

Shipping

The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.

Stability&Storage

Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Reconstitution

Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

 

 

 

Alternative Names

Hepatocyte growth factor receptor; HGF receptor; HGF/SF receptor; Proto-oncogene c-Met; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met; MET

 

Background

Hepatocyte growth factor receptor (HGF R) 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. Mature HGF R is a disulfide-linked dimer composed of a 50 kDa extracellular α chain and a 145 kDa transmembrane β chain. 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 α and β chains. The sema domain, which is formed by both α and β chains of HGF R, mediates both ligand binding and receptor dimerization. HGF stimulation induces HGF R downregulation via internalization and proteasomedependent degradation. 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.

 

Note

For Research Use Only , Not for Diagnostic Use.