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The protein encoded by STRA6 is a membrane protein involved in the metabolism of retinol. Additionally we are shipping STRA6 Antibodies (70) and STRA6 Kits (1) and many more products for this protein.
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These data establish that holo-RBP (show RBP4 Proteins) and its receptor STRA6 are potent oncogenes and suggest that the pathway is a novel target for therapy of some human cancers.
Evidence for the existence of a transmembrane pore, analogous to the pore of ion channels, in STRA6.
STRA6 has a role for regulating retinoid homeostasis and in helping to program signaling that drives proliferation and differentiation of human skin cells
Stra6, a retinoic acid-responsive (show GPRC5A Proteins) gene, participates in p53 (show TP53 Proteins)-induced apoptosis after DNA damage.
Analysis of FRAS1 and STRA6 mutations in the same family with eye anomalies.
Findings suggest that heterozygosity for the STRA6 gene mutation may be associated with ocular abnormalities.
TTR (show TTR Proteins) blocks the ability of holo-retinol-binding protein to associate with STRA6 and thereby effectively suppresses both STRA6-mediated retinol uptake and STRA6-initiated cell signaling.
STRA6 orchestrates a multicomponent machinery that couples vitamin A homeostasis and metabolism to activation of a signaling cascade and that, in turn, STRA6 signaling regulates the cellular uptake of the vitamin.
STRA6 mutations can cause isolated eye malformations in addition to the congenital anomalies observed in MWS.
SNPs in STRA6, gene coding the cell surface receptor for RBP4 (show POLR2D Proteins), were significantly associated with type 2 diabetes and further genetic and functional studies are required to understand and ascertain its role in the manifestation of type 2 diabetes.
Studies indicate that STRA6 is indeed a bona fide vitamin A transporter and provide novel insights into the regulatory mechanism that governs vitamin A homeostasis in peripheral tissues.
Total vitamin A levels are dramatically lower in the eyes of STRA6 KO mice as compared to those of WT mice, but the levels in other organs were not significantly affected after STRA6 deletion under vitamin A sufficient conditions.
STRA6 reduction in adipocytes in adipose-Stra6(-/-) mice.
Rbp4 (show RBP4 Proteins) and its membrane receptor STRA6 control adipogenesis by regulating cellular retinoid homeostasis and RARalpha (show RARA Proteins) activity.
STRA6 in tissues other than the eye appears to be the coupling of circulating holo-RBP (show RBP4 Proteins) levels to cell signaling, in turn regulating key processes such as insulin (show INS Proteins) response.
Stra6, a retinoic acid-responsive gene, participates in p53 (show TP53 Proteins)-induced apoptosis after DNA damage.
LRAT (show LRAT Proteins) acts together with Cyp26A1 (show CYP26A1 Proteins), one of the enzymes that catalyze the degradation of retinoic acid, and possibly with STRA6, the recently identified cell surface receptor for retinol-RBP (show RBP4 Proteins)
STRA6 was identified in retinal pigment epithelium cells as a specific membrane receptor for retinol binding protein (RBP (show RBP4 Proteins)); STRA6 binds to RBP (show RBP4 Proteins) with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP (show RBP4 Proteins) complex
study identifies an essential functional domain in STRA6
The protein encoded by this gene is a membrane protein involved in the metabolism of retinol. The encoded protein acts as a receptor for retinol/retinol binding protein complexes. This protein removes the retinol from the complex and transports it across the cell membrane. Defects in this gene are a cause of syndromic microphthalmia type 9 (MCOPS9). Several transcript variants encoding a few different isoforms have been found for this gene.
stimulated by retinoic acid gene 6 homolog
, stimulated by retinoic acid gene 6 protein homolog
, stimulated by retinoic acid 6 homolog
, retinoic acid-responsive protein
, stimulated by retinoic acid gene 6 protein