Recombinant Human FGF-16
| Code | Size | Price |
|---|
| LEI-F125-25ug | 25 ug | £432.00 |
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 lyophilized from a 0.2 um filtered solution in MOPS, EDTA, Dithiothreitol (DTT), and sodium sulphate (Na2SO4).
Formulation:
This recombinant protein was lyophilized from a 0.2 um filtered solution in MOPS, EDTA, Dithiothreitol (DTT), and sodium sulphate (Na2SO4).
Long Description:
Fibroblast growth factor 16 (FGF-16) is a member of the fibroblast growth factor (FGF) family, which are all heparin-binding growth factors. FGF-16 is most similar to FGF-9 sharing 73% amino acid identity. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-16 is released from neonatal cardiac myocytes and alters growth-related signaling, possibly interfering with cardiac myocyte proliferative potential (2). It lacks a typical signal peptide but is efficiently generated by mechanisms other than the classical protein secretion pathway. FGF-16 signals through the receptors FGFR 2c and 3c (3). It induces proliferation of primary adipocytes and oligodendrocytes in vitro and stimulates liver weight increase in vivo (4).
NCBI Gene:
8823
Purity:
>97% by SDS-PAGE and analyzed by silver stain.
Target:
FGF-16
References
1. Cattini, PA. et al. (2003) Mol. Cell. Biochem. 242:65
2. Lu, SY. et al. (2008) Amer. J. Physiol. 294:1242
3. Zhang, X. et al. (2006) J. Biol. Chem. 281:15694
4. Konishi, M. et al. (2000) J. Biol. Chem. 275:12119
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