Measured by its ability to bind alltrans retinoic acid. The binding of retinoic acid results in the quenching of Trp fluorescence in RBP4. The 50% binding concentration (BC50) is >1 µM

RBP4 Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 22.4 kDa and the accession number is F1PQI4.

Canine

HEK293 Cells

retinol binding protein 4, plasma

A DNA sequence encoding the canine RBP4 (F1PQI4) (Met1-Leu201) was expressed with a C-terminal polyhistidine tag. Predicted N terminal: Glu 19

> 94 % as determined by SDS-PAGE

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Retinol-binding protein 4 (RBP4) is the specific carrier for retinol (also known as vitamin A), and is responsible for the conversion of unstable and insoluble retinol in aqueous solution into stable and soluble complex in plasma through their tight interaction. As a member of the lipocalin superfamily, RBP4 containing a β-barrel structure with a well-defined cavity is secreted from the liver, and in turn delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), and this binding is crucial for preventing RBP4 excretion through the kidney glomeruli. RBP4 expressed from an ectopic source efficiently delivers retinol to the eyes, and its deficiency affects night vision largely. Recently, RBP4 as an adipokine, is found to be expressed in adipose tissue and correlated with obesity, insulin resistance (IR) and type 2 diabetes (T2DM).