Other Proteins

Chemerin is a chemoattractant expressed in white adipose, liver and lung tissues. Chemerin is a ligand for the G-protein coupled receptor known as ChemR23 (or chemokine-like receptor-1), which is expressed mainly on dendritic cells, macrophages and some adipocytes. Recombinant human Chemerin is a non-glycosylated protein, containing 138 amino acids, with a total molecular weight of 16 kDa.

Ciliary Neurotrophic Factor (CNTF) is a neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system. CNTF, like FGF acidic, FGF basic, and PD-ECGF (platelet-derived endothelial cell growth factor), does not possess a signal sequence that would allow secretion of the factor by classical secretion pathways (endoplasmatic reticulum/Golgi system), but the mechanism underlying the release of CNTF is unknown. Recombinant human CNTF is a non-glycosylated protein, contains 199 amino acids, with a molecular weight of 22.7 kDa.

Ciliary Neurotrophic Factor (CNTF) is a neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system. CNTF, like FGF acidic, FGF basic, and PD-ECGF (platelet-derived endothelial cell growth factor), does not possess a signal sequence that would allow secretion of the factor by classical secretion pathways (endoplasmatic reticulum/Golgi system), but the mechanism underlying the release of CNTF is unknown. Recombinant human CNTF is a non-glycosylated protein, contains 199 amino acids, with a molecular weight of 22.7 kDa.

Ciliary Neurotrophic Factor (CNTF) is a neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system. CNTF, like FGF acidic, FGF basic, and PD-ECGF (platelet-derived endothelial cell growth factor), does not possess a signal sequence that would allow secretion of the factor by classical secretion pathways (endoplasmatic reticulum/Golgi system), but the mechanism underlying the release of CNTF is unknown. Recombinant human CNTF is a non-glycosylated protein, contains 199 amino acids, with a molecular weight of 22.7 kDa.

Connective Tissue Growth Factor (CTGF) is a member of cysteine rich regulatory proteins that are both mitogenic and chemotactic. Each protein has an Insulin-like Growth Factor (IGF)-binding domain, a thrombospondin type 1 domain and cysteine knot region. CTGF has multiple effects on development and differentiation. Recombinant human CTGF is a non-glycosylated protein, containing 98 amino acids, with a molecular weight of 11.2 kDa.

Connective Tissue Growth Factor (CTGF) is a member of cysteine rich regulatory proteins that are both mitogenic and chemotactic. Each protein has an Insulin-like Growth Factor (IGF)-binding domain, a thrombospondin type 1 domain and cysteine knot region. CTGF has multiple effects on development and differentiation. Recombinant human CTGF is a non-glycosylated protein, containing 98 amino acids, with a molecular weight of 11.2 kDa.

Connective Tissue Growth Factor (CTGF) is a member of cysteine rich regulatory proteins that are both mitogenic and chemotactic. Each protein has an Insulin-like Growth Factor (IGF)-binding domain, a thrombospondin type 1 domain and cysteine knot region. CTGF has multiple effects on development and differentiation. Recombinant human CTGF is a non-glycosylated protein, containing 98 amino acids, with a molecular weight of 11.2 kDa.

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.

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.