Other Proteins

Recombinant Murine FGF-9 (Legacy Tebubio ref. 167450-30). FGF-9 is a heparin-binding growth factor that belongs to 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-9 targets glial cells, astrocytes cells and other cells that express FGFR 1c, 2c, 3b, 3c, and 4. Recombinant Murine FGF-9 is a 23.3 kDa protein containing 206 amino acid residues.

Recombinant Murine FGF-9 (Legacy Tebubio ref. 167450-30). FGF-9 is a heparin-binding growth factor that belongs to 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-9 targets glial cells, astrocytes cells and other cells that express FGFR 1c, 2c, 3b, 3c, and 4. Recombinant Murine FGF-9 is a 23.3 kDa protein containing 206 amino acid residues.

Recombinant Murine FGF-basic (Legacy Tebubio ref. 167450-33). FGF-basic is one of 23 known members 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-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Murine FGF-basic is a 16.3 kDa protein consisting of 145 amino acid residues.

Recombinant Murine FGF-basic (Legacy Tebubio ref. 167450-33). FGF-basic is one of 23 known members 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-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Murine FGF-basic is a 16.3 kDa protein consisting of 145 amino acid residues.

Recombinant Murine FGF-acidic (Legacy Tebubio ref. 167450-33A). FGF-acidic is one of 23 known members 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-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant Murine FGF-acidic is a 15.9 kDa protein consisting of 141 amino acid residues.

Recombinant Murine FGF-acidic (Legacy Tebubio ref. 167450-33A). FGF-acidic is one of 23 known members 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-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant Murine FGF-acidic is a 15.9 kDa protein consisting of 141 amino acid residues.

Recombinant Murine beta-NGF (Legacy Tebubio ref. 167450-34). Beta-NGF is a neurotrophic factor structurally related to BDNF, NT-3 and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Beta-NGF is a potent neurotrophic factor that signals through its receptor beta-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. Beta-NGF also acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. The functional form of Recombinant Murine beta-NGF is a non-covalently-linked homodimer of two 13.4 kDa, polypeptide monomers that each contain 120 amino acids and three disulfide bonds, which are required for biological activity.

Recombinant Murine beta-NGF (Legacy Tebubio ref. 167450-34). Beta-NGF is a neurotrophic factor structurally related to BDNF, NT-3 and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Beta-NGF is a potent neurotrophic factor that signals through its receptor beta-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. Beta-NGF also acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. The functional form of Recombinant Murine beta-NGF is a non-covalently-linked homodimer of two 13.4 kDa, polypeptide monomers that each contain 120 amino acids and three disulfide bonds, which are required for biological activity.

Recombinant Murine Persephin (Legacy Tebubio ref. 167450-35). Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR alpha (alpha1-alpha4) receptors. The GFRalpha4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Murine Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 total amino acid residues). Each chain contains seven conserved cysteine r