| Reactivity | MuSpecies Glossary |
| Applications | Binding Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to bind all-trans retinoic acid. The binding of retinoic acid results in the quenching of Trp fluorescence in RBP4. <br />The 50% binding concentration (BC<SUB>50</SUB>) is >0.5 µM, as measured under the described conditions. <br /><br /> |
| Accession # | |
| N-terminal Sequence | Glu19 |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | Rbp4 |
| Endotoxin Note | <1.000 EU per 1 µg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 22 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 22 kDa, reducing conditions |
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| Publications |
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| Storage | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
| Buffer | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl. |
| Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile 50 mM Tris, 10 mM CaCl2 and 150 mM NaCl, pH 7.5. |
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.
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