Recombinant Human HGF (NS0 Cell Expressed)
| Code | Size | Price |
|---|
| LEI-H1475-5ug | 5 ug | £420.00 |
Quantity:
| LEI-H1475-100ug | 100 ug | £785.00 |
Quantity:
| LEI-H1475-25ug | 25 ug | £1,866.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Human
Regulatory Status: RUO
Shipping:
Ambient
Storage:
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Further Information
Format:
This recombinant protein was 0.2 um filtered and lyophilized from modified Dulbecco?s phosphate buffered saline (1X PBS) pH 7.2 ? 7.3 with no calcium, magnesium, or preservatives.
Formulation:
This recombinant protein was 0.2 um filtered and lyophilized from modified Dulbecco?s phosphate buffered saline (1X PBS) pH 7.2 ? 7.3 with no calcium, magnesium, or preservatives.
Long Description:
Hepatocyte growth factor/scatter factor (HGF/SF) is a paracrine cellular growth, motility and morphogenic factor. It is secreted by mesenchymal cells and targets and acts primarily upon epithelial cells and endothelial cells, but also acts on haemopoietic progenitor cells. It has been shown to have a major role in embryonic organ development, in adult organ regeneration and in wound healing.1Hepatocyte 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.
NCBI Gene:
3082
Purity:
>95% by SDS-PAGE and analyzed by silver stain.
Target:
HGF
References
1. Lyon, M. et al. (2000) Proteoglycans: structure, biology and molecular interactions.: 27
2. Corso, S. et al. (2005) Trends Mol. Med. 11:284.
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