Species |
Human |
Protein Construction |
RBP4 (Glu19-Leu201) Accession # P02753 |
Poly-His |
N-term |
C-term |
|
Purity |
> 97% as analyzed by SDS-PAGE > 97% as analyzed by HPLC |
Endotoxin Level |
< 0.2 EU/μg of protein by gel clotting method |
Biological Activity |
Measured by its ability to bind all-trans retinoic acid. The binding of retinoic acid results in the quenching of Trp fluorescence in RBP4. > 1.0 µM all-trans retinoic acid is bound under the described conditions. |
Expression System |
HEK 293 |
Apparent Molecular Weight |
~22 kDa, on SDS-PAGE under reducing conditions. |
Formulation |
Lyophilized from a 0.2 μm filtered solution in 50 mM Tris-HCl, 150 mM NaCl, pH 7.5. |
Reconstitution |
It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH₂O or PBS up to 100 μg/ml. |
Storage & Stability |
Upon receiving, this product remains stable for up to 6 months at lower than -70°C. Upon reconstitution, the product should be stable for up to 1 week at 4°C or up to 3 months at -20°C. For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles. |
Target Background |
The properties of retinol binding protein is the transport carrier of vitamin A in the plasma. Human-retinol binding protein is a single-chain polypeptide with a molecular weight of approximately 21000 and one binding site for retinol and other forms of vitamin A. In addition, compounds related to retinol, such as retinal, retinoic acid, retinyl esters and geometric isomers of retinol and of retinal were evaluated for their ability to bind to this protein. In plasma, RBP4-retinol forms a complex with transthyretin (TTR), also known as thyroxine-binding protein and prealbumin. Defects in RBP4 cause retinol-binding protein deficiency, which affects night vision. |
Synonyms |
RBP-4; Retinol-Binding Protein 4 |
For laboratory research use only. Direct human use, including taking orally and injection and clinical use are forbidden.