beta-NGF (human), animal-free recombinant

Product Description: beta-NGF, a neurotrophic factor structurally akin to BDNF, NT-3, and NT-4, is part of the cysteine-knot family of growth factors, characterized by stable dimeric structures. This potent neurotrophic factor operates via its receptor beta-NGFR, playing a pivotal role in the development and maintenance of the sensory and sympathetic nervous systems. Additionally, beta-NGF functions as a growth and differentiation factor for B lymphocytes, boosting B-cell survival. The active form of Recombinant Human beta-NGF is a non-covalently linked homodimer comprising two 13.5 kDa polypeptide monomers, each containing 120 amino acids and three disulfide bonds essential for biological activity. . Amino acid sequence: SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA. Endotoxin concentration: <0.1 EU/µg. Activity: Determined by the dose-dependent stimulation of the proliferation of human TF-1 cells. The expected ED50 is = 1.0 ng/ml, corresponding to a specific activity of > 1 x 10^6 units/mg. Contains no preservative. Protein function: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:14976160, PubMed:20978020). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (PubMed:20978020) (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (PubMed:20164177). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form. [The UniProt Consortium]