Other Proteins

Recombinant Human FGF-21 (Legacy Tebubio ref. 167100-42). FGF-21 is a secreted growth factor that is a member of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-21, in the presence of beta-Klotho as a protein cofactor, signals through the FGFR 1c and 4 receptors, and stimulates insulin-independent glucose uptake by adipocytes. Recombinant Human FGF-21 is a 19.5 kDa protein containing 182 amino acid residues.

Recombinant Human FGF-21 (Legacy Tebubio ref. 167100-42). FGF-21 is a secreted growth factor that is a member of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-21, in the presence of beta-Klotho as a protein cofactor, signals through the FGFR 1c and 4 receptors, and stimulates insulin-independent glucose uptake by adipocytes. Recombinant Human FGF-21 is a 19.5 kDa protein containing 182 amino acid residues.

Recombinant Human EG-VEGF (Legacy Tebubio ref. 167100-44). EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The human EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Human EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Human EG-VEGF (Legacy Tebubio ref. 167100-44). EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The human EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Human EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Human Sonic Hedgehog (Shh) (Legacy Tebubio ref. 167100-45). Members of the Hedgehog (Hh) family are highly conserved proteins that are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh), are structurally related, and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93% identical). The biologically active form of each Hh molecule is obtained by autocatalytic cleavage of their precursor proteins, and each corresponds to approximately one half of the N-terminal portion of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can be substituted for one another in experimental systems. Recombinant E.coli-derived Human Sonic Hedgehog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence s

Recombinant Human Sonic Hedgehog (Shh) (Legacy Tebubio ref. 167100-45). Members of the Hedgehog (Hh) family are highly conserved proteins that are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh), are structurally related, and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93% identical). The biologically active form of each Hh molecule is obtained by autocatalytic cleavage of their precursor proteins, and each corresponds to approximately one half of the N-terminal portion of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can be substituted for one another in experimental systems. Recombinant E.coli-derived Human Sonic Hedgehog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence s

Recombinant Human Prokineticin-2 (Legacy Tebubio ref. 167100-46). Prokineticin-2 (PK2) is a cysteine-rich secreted protein that is expressed in the testis and, in lower levels, in the small intestine. PK2 regulates various biological functions, including gastrointestinal motility, angiogenesis and circadian rhythms. It is closely related to EG-VEGF (Prokineticin-1), and binds to two orphan B-protein-coupled receptors termed PK-R1 and PK-R2. Recombinant Human Prokineticin-2 is an 8.8 kDa protein consisting of 81 amino acid residues, including ten cysteine residues that can potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Human Prokineticin-2 (Legacy Tebubio ref. 167100-46). Prokineticin-2 (PK2) is a cysteine-rich secreted protein that is expressed in the testis and, in lower levels, in the small intestine. PK2 regulates various biological functions, including gastrointestinal motility, angiogenesis and circadian rhythms. It is closely related to EG-VEGF (Prokineticin-1), and binds to two orphan B-protein-coupled receptors termed PK-R1 and PK-R2. Recombinant Human Prokineticin-2 is an 8.8 kDa protein consisting of 81 amino acid residues, including ten cysteine residues that can potentially form five pairs of intra-molecular disulfide bonds.

Recombinant Human HB-EGF (Legacy Tebubio ref. 167100-47). HB-EGF is an EGF-related growth factor that signals through the EGF receptor, and stimulates the proliferation of smooth muscle cells (SMC), fibroblasts, epithelial cells, and keratinocytes. HB-EGF is expressed in numerous cell types and tissues, including vascular endothelial cells, and vascular SMC, macrophages, skeletal muscle, keratinocytes, and certain tumor cells. The ability of HB-EGF to specifically bind heparin and heparin sulfate proteoglycans is distinct from other EGF-like molecules, and may be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells. The human HB-EGF gene encodes a 208 amino acid transmembrane protein, which can be proteolytically cleaved to produce soluble HB-EGF. Recombinant Human HB-EGF is a 9.7 kDa protein containing 86 amino acid residues, corresponding to the extracellular EGF-like and heparin-binding domains of the full length HB-EGF protein.