GenScript Biotech

Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients.The cDNAs for EPO have been cloned from human, mouse, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.

Epiregulin is a member of the EGF family of growth factors which includes, among others, epidermal growth factor (EGF), transforming growth factor (TGF)-alpha, amphiregulin (ARG), HB (heparin-binding)-EGF, betacellulin, and the various heregulins. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Epiregulin is a member of the EGF family of growth factors which includes, among others, epidermal growth factor (EGF), transforming growth factor (TGF)-alpha, amphiregulin (ARG), HB (heparin-binding)-EGF, betacellulin, and the various heregulins. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Exendin-4 is a novel 39-amino acid peptide isolated from the venom of the Gila monster Heloderma suspectum. It shares 53% sequence homology with GLP-17-36amide and interacts with the same membrane receptor. Exendin-4 enhances glucose-dependent insulin secretion, suppresses inappropriately elevated glucagon secretion, and slows gastric emptying in vivo. It also promotes ß-cell proliferation and neogenesis in vitro and in animal models.

Exendin-4 is a novel 39-amino acid peptide isolated from the venom of the Gila monster Heloderma suspectum. It shares 53% sequence homology with GLP-17-36amide and interacts with the same membrane receptor. Exendin-4 enhances glucose-dependent insulin secretion, suppresses inappropriately elevated glucagon secretion, and slows gastric emptying in vivo. It also promotes ß-cell proliferation and neogenesis in vitro and in animal models.

Exodus-2/CCL21 is a novel CC chemokine discovered independently by three groups from the EST database, and shows 21-33% identity to other CC chemokines. Exodus-2 contains the four conserved cysteines characteristic of β chemokines plus two additional cysteines in its unusually long carboxyl terminal domain. It is expressed in lymph nodes of certain endothelial cells, and in the spleen and appendix. Exodus-2 chemoattracts T and B lymphocytes and inhibits hematopoiesis.

Exodus-2/CCL21 is a novel CC chemokine discovered independently by three groups from the EST database, and shows 21-33% identity to other CC chemokines. Exodus-2 contains the four conserved cysteines characteristic of β chemokines plus two additional cysteines in its unusually long carboxyl terminal domain. It is expressed in lymph nodes of certain endothelial cells, and in the spleen and appendix. Exodus-2 chemoattracts T and B lymphocytes and inhibits hematopoiesis.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in the lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF and receptor binding to FGFR2-IIIb. However, while KGF induces proliferation and differentiation of various epithelial cells, FGF-10 promotes budding and branching morphogenesis during the multi-organ development via mesenchymal-epithelial cell interactions. FGF-10 is critical for lung and limb development, and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in the lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF and receptor binding to FGFR2-IIIb. However, while KGF induces proliferation and differentiation of various epithelial cells, FGF-10 promotes budding and branching morphogenesis during the multi-organ development via mesenchymal-epithelial cell interactions. FGF-10 is critical for lung and limb development, and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in the lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF and receptor binding to FGFR2-IIIb. However, while KGF induces proliferation and differentiation of various epithelial cells, FGF-10 promotes budding and branching morphogenesis during the multi-organ development via mesenchymal-epithelial cell interactions. FGF-10 is critical for lung and limb development, and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF, and both KGF and FGF-10 activate the receptor FGFR2-IIIb. However, unlike KGF, which induces the proliferation and differentiation of various epithelial cells, FGF-10 is an essential factor for the budding and branching morphogenesis during multi-organ development via mesenchymal-epithelial interactions. FGF-10 is crucial for lung and limb development and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF, and both KGF and FGF-10 activate the receptor FGFR2-IIIb. However, unlike KGF, which induces the proliferation and differentiation of various epithelial cells, FGF-10 is an essential factor for the budding and branching morphogenesis during multi-organ development via mesenchymal-epithelial interactions. FGF-10 is crucial for lung and limb development and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF, and both KGF and FGF-10 activate the receptor FGFR2-IIIb. However, unlike KGF, which induces the proliferation and differentiation of various epithelial cells, FGF-10 is an essential factor for the budding and branching morphogenesis during multi-organ development via mesenchymal-epithelial interactions. FGF-10 is crucial for lung and limb development and is regulated by Shh during early development.

Fibroblast Growth Factor 12 (FGF-12) is a member of the fibroblast growth factor (FGF) family. FGF-12 is probably involved in nervous system development and function. FGF-12 lacks the N-terminal signal sequence present in most of the FGF family members, but it contains clusters of basic residues that have been demonstrated to act as a nuclear localization signal. When transfected into mammalian cells, this protein accumulated in the nucleus, but was not secreted. The specific function of this gene has not yet been determined. Two alternatively spliced transcript variants encoding distinct isoforms have been reported.

Fibroblast Growth Factor 12 (FGF-12) is a member of the fibroblast growth factor (FGF) family. FGF-12 is probably involved in nervous system development and function. FGF-12 lacks the N-terminal signal sequence present in most of the FGF family members, but it contains clusters of basic residues that have been demonstrated to act as a nuclear localization signal. When transfected into mammalian cells, this protein accumulated in the nucleus, but was not secreted. The specific function of this gene has not yet been determined. Two alternatively spliced transcript variants encoding distinct isoforms have been reported.

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. 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. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. 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. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. 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. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.

Fibroblast Growth Factor-18 (FGF-18) is a heparin-binding growth factor that is a member of the FGF family. FGF-18 signals through FGFR 1c, 2c, 3c, and 4. FGF-18 plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. FGF-18 is required for normal ossification and bone development. It can also stimulate hepatic and intestinal proliferation.

Fibroblast Growth Factor-18 (FGF-18) is a heparin-binding growth factor that is a member of the FGF family. FGF-18 signals through FGFR 1c, 2c, 3c, and 4. FGF-18 plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. FGF-18 is required for normal ossification and bone development. It can also stimulate hepatic and intestinal proliferation.

Fibroblast Growth Factor-18 (FGF-18) is a heparin-binding growth factor that is a member of the FGF family. FGF-18 signals through FGFR 1c, 2c, 3c, and 4. FGF-18 plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. FGF-18 is required for normal ossification and bone development. It can also stimulate hepatic and intestinal proliferation.

Murine FGF-18 is encoded by the FGF18 gene. By phylogenetic analysis and gene location analysis, FGF-18 is divided into FGF-8 subfamily which has three members FGF-8, FGF-17 and FGF-18. Using FGF knockout mice model, the numbers of this subfamily were testified that have crucial roles in embryo development. FGF-18–/– mice have decreased expression of osteogenic markers and delayed long-bone ossification. FGF-18 has been shown in vitro that this protein is able to induce neurite outgrowth in PC12 cells. In addition, it also has significant roles in lung development and has an anabolic effect on cartilage formation.

Murine FGF-18 is encoded by the FGF18 gene. By phylogenetic analysis and gene location analysis, FGF-18 is divided into FGF-8 subfamily which has three members FGF-8, FGF-17 and FGF-18. Using FGF knockout mice model, the numbers of this subfamily were testified that have crucial roles in embryo development. FGF-18–/– mice have decreased expression of osteogenic markers and delayed long-bone ossification. FGF-18 has been shown in vitro that this protein is able to induce neurite outgrowth in PC12 cells. In addition, it also has significant roles in lung development and has an anabolic effect on cartilage formation.

Fibroblast Growth Factor 18 (FGF-18) is a pleiotropic cytokine belonging to the heparin-binding FGF family, which has 23 different members. Structurally, FGF-18 is closely related to FGF-8 and FGF-17. Like other FGFs, FGF-18 can bind to different FGF receptors in vivo. FGF-18 is expressed in various tissues and has multiple functions: during long bone growth, FGF-18 is expressed in perichondrium and developing joints, and regulates bone formation by inhibiting chondrocyte proliferation and differentiation; FGF-18 knock-out mice survive embryonic development, but exhibit skeletal abnormalities and die in the early neonatal period. FGF-18 also induces ectopic cartilage formation in the lung, and alters the morphology of the pulmonary mesenchyma.