Recombinant human IGFBP5 produced in
E. coli is non-glycosylated homodimer containing 2x252 amino acids and having a molecular mass of 28.6 kDa. IGFBP5 is purified by proprietary chromatographic techniques.
Synonyms: IGFBP-5, IBP-5, IGF-binding protein 5.
Formulation: IBP-5 was lyophilized from a concentrated (1mg/ml) solution containing 10 mM sodium Citrate pH -3.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Purity: Greater than 96.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Source:Escherichia coli. Amino acid sequence: LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
Uniprot ACC number: P24593
Transportation method: Shipped at room temperature.
Stability: Lyophilized IBP5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP 5 should be stored at +4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Biological Activity: The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4 µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15 ng/ml of rHuIGF-II.
Solubility: It is recommended to reconstitute the lyophilized Insulin-Like Growth Factor Binding Protein-5 in sterile 18MΩ-cm H
2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
References: Title:Effects of Dietary Carbohydrate Modificationin Persons with the Metabolic Syndrome- A Transcriptomics Approach in Adipose TissuePublication:Department of Clinical Nutrition, Food and Health Research CentreInstitute of Public Health and Clinical NutritionFaculty of Health SciencesUniversity of Eastern Finland Kuopio 2010Link:http://epublications. uef. fi/pub/urn_isbn_978-952-61-0024-1/urn_isbn_978-952-61-0024-1. pdf
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