|Detection of Human RBP4/Retinol‑Binding Protein 4 by Western Blot. Western blot shows lysates of human liver tissue, and human serum. PVDF membrane was probed with 0.1 µg/mL of Rat Anti-Human/Mouse RBP4/Retinol‑Binding Protein 4 Monoclonal Antibody (Catalog # MAB34762) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for RBP4/Retinol‑Binding Protein 4 at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Retinol (also known as vitamin A) is unstable and insoluble in the aqueous solution. However, retinol becomes quite stable and soluble in plasma due to its tight interaction with Retinol-binding Protein 4 (RBP4), also known as Plasma Retinol-binding Protein (1‑3). A prototypic member of the lipocalin superfamily, RBP4 has a beta ‑barrel structure with a well-defined cavity. It is secreted from the liver, a process requiring the availability of retinol. RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. The retinol-RBP4-TTR complex prevents the loss of RBP4 by filtration through the kidney and increases the stability of the retinol-RBP4 complex. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision. Serum RBP4 levels are elevated in insulin-resistant mice and humans with obesity and type 2 diabetes, implying that RBP4, an adipocyte-derived signal, may be a biomarker and a drug target for the two diseases. The amino acid sequence of mouse RBP4 is 99%, 86%, 83% and 75% identical to that of rat, human/chimpanzee, dog and chicken.
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