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Retinol Binding Protein

16-16-180216
Athens Research
Protein IDP02753
Product group Proteins / Signaling Molecules
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Overview

  • Supplier
    Athens Research
  • Product Name
    Retinol Binding Protein
  • Delivery Days Customer
    9
  • Applications Supplier
    In Vitro Diagnostics, Diabetes, Inflammation, Cardiovascular Disease, Biotherapeutics
  • Certification
    Research Use Only
  • Estimated Purity
    ≥95% by SDS-PAGE.
  • Protein IDP02753
  • Protein Name
    Retinol-binding protein 4
  • Scientific Description
    Retinol binding protein 4 (RBP4) is a member of the lipocalin family and serves as the primary transporter of retinol (vitamin A) in the bloodstream, present at about 40 mg/L in healthy individuals. Synthesized mainly in the liver, RBP4 binds retinol and forms a complex with transthyretin, which prevents its loss via kidney filtration and ensures efficient delivery of vitamin A to peripheral tissues. Beyond its canonical role in retinoid homeostasis, RBP4 functions as an adipokine and has been implicated in metabolic regulation. Elevated RBP4 levels are strongly associated with insulin resistance, obesity, type 2 diabetes, gestational diabetes, metabolic syndrome, and cardiovascular diseases, correlating with increased levels of APO B-containing lipoproteins such as LDL and VLDL. RBP4 can also trigger adipose tissue inflammation, linking it to chronic metabolic and inflammatory conditions. Clinically, RBP4 is under investigation as a biomarker for metabolic disorders and chronic kidney disease, and as a potential therapeutic target in diabetes and cardiovascular risk management.
  • Shelf life instruction
    more then 1 year
  • Source
    Source human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
  • Storage Instruction
    ≤ -20°C
  • UNSPSC
    12352202

References

  • Est., C. B., et al., (2020), 'Retinol binding protein IV purified from Escherichia coli using intein-mediated cleavage as a suitable replacement for serum sources', Protein Expression and Purification. 167: p 105542
    Read this paper
  • Zheng, Y. Z., et al., (2017), 'Manipulating trypsin digestion conditions to accelerate proteolysis and simplify digestion workflows in development of protein mass spectrometric assays for the clinical laboratory,' Clinical Mass Spectrometry 6: pp 1–12
    Read this paper