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The results provide evidence for an exclusive proteasome subunit-related mechanism for transcriptional activation of RBP4 (show RBP4 Proteins) within a GLUT4 (show SLC2A4 Proteins) knockdown model.
demonstrated that retinol bound to CRBP-III is an excellent substrate for lecithin-retinol acyltransferase (show LRAT Proteins), the enzyme responsible for catalyzing retinyl ester formation from retinol
CRBP-III is a PPARgamma (show PPARG Proteins) target gene and plays a role in lipid and whole body energy metabolism.
Human CRBP (show RBP1 Proteins) IV belongs to a clearly distinct CRBP (show RBP1 Proteins) subfamily and suggest a relatively different mode of retinol binding for this binding protein.
Due to its chemical instability and low solubility in aqueous solution, vitamin A requires cellular retinol-binding proteins (CRBPs), such as RBP7, for stability, internalization, intercellular transfer, homeostasis, and metabolism.
retinoid-binding protein 7
, retinol binding protein 7, cellular
, DNA-directed RNA polymerase II subunit G
, DNA-directed RNA polymerase II subunit RPB7
, RNA polymerase II subunit B7
, cellular retinoic acid-binding protein 4
, cellular retinoic acid-binding protein IV
, putative cellular retinol-binding protein CRBP IV
, retinoid binding protein 7
, cellular retinol binding protein type III
, cytosolic binding protein