Other Proteins

Endocrine Gland-derived Vascular Endothelial Growth Factor (EG-VEGF) is an angiogenic growth factor specifically expressed in the ovaries, testis, adrenal and placental tissues. The identification of tissue-selective angiogenic factors raises the possibility that other secreted molecules in this class exist. EG-VEGF expression correlates with vascularity in polycystic ovary syndrome, a leading cause of infertility. Recombinant human EG-VEGF is a non-glycosylated protein, containing 86 amino acids, with a molecular weight of 9.6 kDa.

Fibroblast Growth Factor 4 (FGF-4) is a growth factor predominantly expressed during embryonic development, playing a key role in limb development. In culture, FGF-4 has been shown to be an important regulator of growth for stem cells, fibroblasts and endothelial cells. Unglycosylated FGF-4 is N-terminally cleaved into 13 kDa or 15 kDa proteins that are more active than the precursor 19 kDa protein, Bellosa P, et al. (1993). Human FGF-4 shares high homology and cross-reactivity with the mouse protein. Recombinant human FGF-4 is a non-glycosylated protein containing 140 amino acids, with a total molecular weight of 15 kDa.

Fibroblast Growth Factor 4 (FGF-4) is a growth factor predominantly expressed during embryonic development, playing a key role in limb development. In culture, FGF-4 has been shown to be an important regulator of growth for stem cells, fibroblasts and endothelial cells. Unglycosylated FGF-4 is N-terminally cleaved into 13 kDa or 15 kDa proteins that are more active than the precursor 19 kDa protein, Bellosa P, et al. (1993). Human FGF-4 shares high homology and cross-reactivity with the mouse protein. Recombinant human FGF-4 is a non-glycosylated protein containing 140 amino acids, with a total molecular weight of 15 kDa.

Fibroblast Growth Factor 4 (FGF-4) is a growth factor predominantly expressed during embryonic development, playing a key role in limb development. In culture, FGF-4 has been shown to be an important regulator of growth for stem cells, fibroblasts and endothelial cells. Unglycosylated FGF-4 is N-terminally cleaved into 13 kDa or 15 kDa proteins that are more active than the precursor 19 kDa protein, Bellosa P, et al. (1993). Human FGF-4 shares high homology and cross-reactivity with the mouse protein. Recombinant human FGF-4 is a non-glycosylated protein containing 140 amino acids, with a total molecular weight of 15 kDa.

Fibroblast Growth Factors (FGFs) are a 22 member family of proteins known to be involved in angiogenesis, wound healing and embryonic development. As a family, they bind to heparin and signal through four receptor tyrosine kinases called, FGFR1, 2, 3 and 4. FGF-21 is most closely related to FGF-19 and shows low binding to heparin and is highly diffusible. Recombinant human FGF-21 is a non-glycosylated protein, containing 182 amino acids, with a molecular weight of 19.5 kDa.

Fibroblast Growth Factors (FGFs) are a 22 member family of proteins known to be involved in angiogenesis, wound healing and embryonic development. As a family, they bind to heparin and signal through four receptor tyrosine kinases called, FGFR1, 2, 3 and 4. FGF-21 is most closely related to FGF-19 and shows low binding to heparin and is highly diffusible. Recombinant human FGF-21 is a non-glycosylated protein, containing 182 amino acids, with a molecular weight of 19.5 kDa.

Fibroblast Growth Factors (FGFs) are a 22 member family of proteins known to be involved in angiogenesis, wound healing and embryonic development. As a family, they bind to heparin and signal through four receptor tyrosine kinases called, FGFR1, 2, 3 and 4. FGF-21 is most closely related to FGF-19 and shows low binding to heparin and is highly diffusible. Recombinant human FGF-21 is a non-glycosylated protein, containing 182 amino acids, with a molecular weight of 19.5 kDa.

Fibroblast Growth Factors (FGFs) are a 22 member family of proteins known to be involved in angiogenesis, wound healing and embryonic development. As a family, they bind to heparin and signal through four receptor tyrosine kinases called, FGFR1, 2, 3 and 4. FGF-21 is most closely related to FGF-19 and shows low binding to heparin and is highly diffusible. Recombinant human FGF-21 is a non-glycosylated protein, containing 182 amino acids, with a molecular weight of 19.5 kDa.

Fibroblast Growth Factors (FGFs) are a 22 member family of proteins known to be involved in angiogenesis, wound healing and embryonic development. As a family, they bind to heparin and signal through four receptor tyrosine kinases called, FGFR1, 2, 3 and 4. Human FGF-22 is a member of the FGF-7 subfamily and is synthesized by multiple cell lines including neurons, keratinocytes and skeletal muscle myotubes. Human FGF-22 shares 86% homology with mouse FGF-22. Recombinant human FGF-22 is a non-glycosylated protein, containing149 amino acids, with a molecular weight of 17.3 kDa.