Recombinant Human HGF (NS0 Expressed) Protein, CF
Recombinant Human HGF (NS0 Expressed) Protein, CF Summary
Gln32-Arg494 alpha chain & Val495-Ser728 beta chain
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS and NaCl with Trehalose.|
|Reconstitution||Reconstitute 10 μg size at 100 μg/mL in PBS. Reconstitute all the other sizes at 200 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.
Recombinant Human HGF induces IL-11 secretion by Saos-2 human osteosarcoma cells. The ED50 for this effect is equal to or less than 4.00 ng/mL.
2 μg/lane of Recombinant Human HGF (NSO Expressed) Protein (Catalog # 11352-HG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 30-40 kDa ( beta chain) & 54-66 kDa ( alpha chain), under reducing conditions.
HGF, also known as scatter factor and hepatopoietin A, is a pleiotropic protein in the plasminogen subfamily of S1 peptidases. It is a multidomain molecule that includes an N-terminal PAN/APPLE‑like domain, four Kringle domains, and a serine proteinase-like domain that has no detectable protease activity (1‑5). Human HGF is secreted as an inactive 728 amino acid (aa) single chain propeptide. It is cleaved after the fourth Kringle domain by a serine protease to form bioactive disulfide‑linked HGF with a 60 kDa alpha and 30 kDa beta chain. Alternate splicing generates human HGF isoforms that lack the proteinase‑like domain and different numbers of the Kringle domains. Human HGF shares 91%‑94% aa sequence identity with bovine, canine, feline, mouse, and rat HGF. HGF binds heparan-sulfate proteoglycans and the widely expressed receptor tyrosine kinase, HGF R/c-MET (6, 7). HGF-dependent c-MET activation is implicated in the development of many human cancers (8). HGF regulates epithelial morphogenesis by inducing cell scattering and branching tubulogenesis (9, 10). HGF induces the up‑regulation of integrin alpha 2 beta 1 in epithelial cells by a selective increase in alpha 2 gene transcription (11). This integrin serves as a collagen I receptor, and its blockade disrupts epithelial cell branching tubulogenesis (11, 12). HGF can also alter epithelium morphology by the induction of nectin‑1 alpha ectodomain shedding, an adhesion protein component of adherens junctions (13). In the thyroid, HGF induces the proliferation, motility, and loss of differentiation markers of thyrocytes and inhibits TSH‑stimulated iodine uptake (14). HGF promotes the motility of cardiac stem cells in damaged myocardium (15).
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