Recombinant Human IGF-BP5 0 ReviewsSubmit a Review Product Details Catalogue Number: 100-05 Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP5 is a 28.6 kDa, cysteine-rich, secreted protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone tissue and helps potentiate the action of IGF-I on smooth muscle cells, fibroblasts, and osteoblasts. Data shows that IGFBP-5 acts as a growth inhibitor and pro-apoptotic agent in breast cancer cells. IGFBP-5-overexpressing mice show an increase in neonatal mortality, reduced female fertility, whole-body growth inhibition, and retarded muscle development. Recombinant Human IGF-BP5 is a 28.6 kDa protein consisting of 253 amino acid residues. Source: E.coli Synonyms: Insulin-like Growth Factor-Binding Protein 5, IBP-5 AA Sequence: MLGSFVHCEP CDEKALSMCP PSPLGCELVK EPGCGCCMTC ALAEGQSCGV YTERCAQGLR CLPRQDEEKP LHALLHGRGV CLNEKSYREQ VKIERDSREH EEPTTSEMAE ETYSPKIFRP KHTRISELKA EAVKKDRRKK LTQSKFVGGA ENTAHPRIIS APEMRQESEQ GPCRRHMEAS LQELKASPRM VPRAVYLPNC DRKGFYKRKQ CKPSRGRKRG ICWCVDKYGM KLPGMEYVDG DFQCHTFDSS NVS Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses. Biological Activity: The ED50 was determined by its ability to inhibit IGF-II induced proliferation of MCF-7 is ≤ 0.3 μg/ml in the presence of 15 ng/ml of human IGF-II. Calculated Molecular Weight: 28.6 kDa Accession Number: P24593 Gene ID: 3488 Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug) crossreactivity: Human References PubMed SDS CoA Search Product Line Country Of Origin: USA Not for human use. Research Interest Apoptosis Cancer Diabetes/Weight Regulation product.subtitle.recentcitations First Author Yamada, K Title Cell surface localization of importin α1/KPNA2 affects cancer cell proliferation by regulating FGF1 signalling. Citation Scientific Reports; 6 pg21410 PubMed Id 26887791 First Author Martino, M M Title Heparin-binding domain of fibrin(ogen) binds growth factors and promotes tissue repair when incorporated within a synthetic matrix. Citation Proceedings of the National Academy of Sciences of the United States of America; 110(12) pg4563-8 PubMed Id 23487783 First Author Francischetti, I M Title Cyr61/CCN1 displays high-affinity binding to the somatomedin B(1-44) domain of vitronectin. Citation PLoS ONE; 5(2) pge9356 PubMed Id 20195466
