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Serum Retinol Binding Protein 4 (human recombinant)

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    Serum Retinol Binding Protein 4 (human recombinant)
  • Serum Retinol Binding Protein 4 (human recombinant)
Cat No: 10007818
Proteins - More Proteins
Cayman

Human serum retinol binding protein 4 (sRBP4) binds to one equivalent of vitamin A and is one of the major retinol carriers found in the blood of mammals.{14372,14373} Human sRBP4 is a monomeric 21 kDa β-sheet-rich protein that contains three disulfid...

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: 100 µg

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • proteins vitamin A blood mammals .beta.-sheet-rich lipocalins hepatocytes plasma tetrameric transthyretin TTR adipocyte-derived adipocytes signaling type 2 diabetes insulin C-terminal terminus hexahistidine tag endocrinology
Product Overview:
Human serum retinol binding protein 4 (sRBP4) binds to one equivalent of vitamin A and is one of the major retinol carriers found in the blood of mammals.{14372,14373} Human sRBP4 is a monomeric 21 kDa β-sheet-rich protein that contains three disulfide bonds and belongs to the lipocalin protein family.{14379} In plasma, sRBP4 typically forms a 1:1 complex with the 55 kDa tetrameric protein transthyretin (TTR) which prevents RBP from being removed from the plasma by glomerular filtration.{14378} Recent studies have shown that sRBP4 is an adipocyte-derived “signal” that may contribute to the pathogenesis of type 2 diabetes.{14371,14380} Elevation of sRBP4 causes systemic insulin resistance, whereas reduced serum concentrations of sRBP4 improves insulin action.{14371,14376,14374} Cayman’s human recombinant sRBP4 contains a C-terminal hexahistidine tag. The purified protein was characterized for its retinol binding activity.
Size 100 µg
Shipping dry ice
Formulation 50 mM sodium phosphate, pH 8.2, with 100 mM sodium chloride and 20% glycerol
Purity ≥95%
Custom Code 3504.00
UNSPSC code 12352202

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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