Recombinant Human Pleiotrophin 0 ReviewsSubmit a Review Product Details Catalogue Number: 450-15 Description: Pleiotrophin and Midkine are structurally related heparin-binding neurotrophic factors, whose expression is developmentally regulated. The expression pattern of these neurotrophic factors suggests function in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm epithelial interaction. The expression of PTN increases during the process of brain embryogenesis, and reaches maximum levels at time of birth. The physiological roles of PTN and Midkine are largely unknown, but these neurotrophins have been implicated in the pathogenesis of neuroblastomas. Recombinant Human Pleiotrophin is a 15.4 kDa protein containing 136 amino acid residues and five intra-molecular disulfide bonds. Source: E.coli Synonyms: PTN, Heparin Affin Regulatory Protein (HARP), Heparin-binding growth factor-8(HBGF-8), Osteoblast-Specific Factor-1 (OSF-1) AA Sequence: GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses. Biological Activity: Not available. Calculated Molecular Weight: 15.4 kDa Accession Number: P21246 Gene ID: 5764 crossreactivity: Bacteria, Chicken, Hamster, Human, Mouse, Rat References PubMed SDS CoA Search Product Line Country Of Origin: USA Not for human use. Research Interest Neurobiology Stem Cells & Differentiation product.subtitle.recentcitations First Author Koutsioumpa, M Title Interplay between αvβ3 integrin and nucleolin regulates human endothelial and glioma cell migration. Citation The Journal of Biological Chemistry; 288(1) pg343-54 PubMed Id 23161541 First Author Li, J Title The pro-angiogenic cytokine pleiotrophin potentiates cardiomyocyte apoptosis through inhibition of endogenous AKT/PKB activity. Citation The Journal of Biological Chemistry; 282(48) pg34984-93 PubMed Id 17925408 First Author Svensson, S L Title Midkine and pleiotrophin have bactericidal properties: preserved antibacterial activity in a family of heparin-binding growth factors during evolution. Citation The Journal of Biological Chemistry; 285(21) pg16105-15 PubMed Id 20308059
