Recombinant Human NT-4 Protein

Description :
FAQ COA 已发表文献 Neurotrophin-4 (NT-4), is a member of the NGF family of neuronal and epithelial growth factors. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds.Mature human NT-4 shares 91% and 95% aa sequence identity with mouse and rat NT-4/5, respectively. The mature protein is secreted as a homodimer and can also form heterodimers with BDNF or NT-3. NT-4 binds and induces receptor dimerization and activation of TrkB. NT-4 promotes the development and survival of selected peripheral and CNS neurons. Product Properties Synonyms Neurotrophin-5, NT-5; Neurotrophin-4 ;GLC10 Accession P34130 GeneID 4909 Source E.coli-derivedHuman NT-4, G81-A210, with an N-terminal Met. Molecular Weight Approximately 28.1kDa. AA Sequence MGVSETAPAS RRGELAVCDA VSGWVTDRRT AVDLRGREVE VLGEVPAAGG SPLRQYFFET RCKADNAEEG GPGAGGGGCR GVDRRHWVSE CKAKQSYVRA LTADAQGRVG WRWIRIDTAC VCTLLSRTGR A Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50as determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures is less than 50 ng/mL, corresponding to a specific activity of > 2.0 104IU/mg.Fully biologically active when compared to standard. Endotoxin 1.0EU per 1g of the protein by the LAL method. Formulation Lyophilized from a 0.2 m filtered concentrated solution in PBS, pH 5.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1%BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at -20. Further dilutions should be made in appropriate buffered solutions.