Thermo Fisher Scientific Human HGF Recombinant Protein

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

-

Immunohistochemistry (IHC)

Assay-dependent

-

ELISA (ELISA)

Assay-dependent

-

Functional Assay (Functional)

Assay-dependent

View 5 publications 5 publications

Control (Ctrl)

Assay-dependent

-

Product Specifications

Species

Human

Published species

Human

Expression System

Insect cells

Amino acid sequence

Human HGF recombinant protein is a heterodimer consisting of a 463 amino acid alpha chain and a 234 amino acid beta chain

Molecular weight

70 kDa

Class

Recombinant

Type

Protein

Purity

>98% by SDS-PAGE

Endotoxin concentration

<0.1 ng/µg

Activity

ED50 = 1 - 20 ng/mL; determined by the dose-dependent proliferation of monkey 4MBr-5 cells.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Storage buffer

PBS

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Wet ice (domestic); Wet or Dry ice (international)

Product Specific Information

Carrier-Free

Source: (BTI-Tn-5B1-4) Hi-5 Insect cells

Reconstitution: Centrifuge the vial briefly, before opening to bring the contents to the bottom. Reconstitute the lyophilized protein in sterile PBS containing 0.1% human serum albumin. Make any further dilutions of the reconstituted protein in low endotoxin medium or a buffered solution containing a carrier protein such as heat inactivated FCS or tissue culture grade BSA.

Storage: Store the lyophilized protein at ≤-20°C, preferably desiccated. Upon reconstitution, apportion into working aliquots and store at ≤-20°C. Avoid repeated freeze-thaw cycles.

Target Information

Hepatocyte growth factor regulates cell growth, cell motility, and morphogenesis by activating a tyrosine kinase signaling cascade after binding to the proto-oncogenic c-Met receptor. Hepatocyte growth factor is secreted by mesenchymal cells and acts as a multi-functional cytokine on cells of mainly epithelial origin. Its ability to stimulate mitogenesis, cell motility, and matrix invasion gives it a central role in angiogenesis, tumorogenesis, and tissue regeneration. It is secreted as a single inactive polypeptide and is cleaved by serine proteases into a 69-kDa alpha-chain and 34-kDa beta-chain. A disulfide bond between the alpha and beta chains produces the active, heterodimeric molecule. The protein belongs to the plasminogen subfamily of S1 peptidases but has no detectable protease activity. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.