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11-cis Retinol Sale

(Synonyms: 11-cis Vitamin A Alcohol) 目录号 : GC48821

An isomer of vitamin A

11-cis Retinol Chemical Structure

Cas No.:22737-96-8

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1mg
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产品描述

11-cis Retinol is an isomer of vitamin A . It is formed from vitamin A, via a trans-retinyl ester intermediate, by the enzyme RPE65 in the retinal pigment epithelium and then converted to 11-cis retinal as part of the visual cycle.1,2 11-cis Retinol is an agonist of salamander and human red rod opsins expressed in COS cells and an inverse agonist of salamander red cone opsin, as well as human red and green cone opsins expressed in COS cells.3 It promotes pigment formation in cone, but not rod, photoreceptors.

1.Rando, R.R.The biochemistry of the visual cycleChem. Rev.101(7)1881-1896(2001) 2.Guignard, T.J.P., Jin, M., Pequignot, M.O., et al.FATP1 inhibits 11-cis retinol formation via interaction with the visual cycle retinoid isomerase RPE65 and lecithin: Retinol acyltransferaseJ. Biol. Chem.285(24)18759-18768(2010) 3.Ala-Laurila, P., Cornwall, M.C., Crouch, R.K., et al.The action of 11-cis-retinol on cone opsins and intact cone photoreceptorsJ. Biol. Chem.284(24)16492-16500(2009)

Chemical Properties

Cas No. 22737-96-8 SDF
别名 11-cis Vitamin A Alcohol
Canonical SMILES OC/C=C(C)/C=C\C=C(C)\C=C\C1=C(C)CCCC1(C)C
分子式 C20H30O 分子量 286.5
溶解度 Chloroform: slightly soluble,Methanol: slightly soluble 储存条件 -80°C
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10 mM 0.349 mL 1.7452 mL 3.4904 mL
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Research Update

FATP1 inhibits 11-cis Retinol formation via interaction with the visual cycle retinoid isomerase RPE65 and lecithin:retinol acyltransferase

J Biol Chem 2010 Jun 11;285(24):18759-68.PMID:20356843DOI:10.1074/jbc.M109.064329.

The isomerization of all-trans retinol (vitamin A) to 11-cis Retinol in the retinal pigment epithelium (RPE) is a key step in the visual process for the regeneration of the visual pigment chromophore, 11-cis retinal. LRAT and RPE65 are recognized as the minimal isomerase catalytic components. However, regulators of this rate-limiting step are not fully identified and could account for the phenotypic variability associated with inherited retinal degeneration (RD) caused by mutations in the RPE65 gene. To identify new RPE65 partners, we screened a porcine RPE mRNA library using a yeast two-hybrid assay with full-length human RPE65. One identified clone (here named FATP1c), containing the cytosolic C-terminal sequence from the fatty acid transport protein 1 (FATP1 or SLC27A1, solute carrier family 27 member 1), was demonstrated to interact dose-dependently with the native RPE65 and with LRAT. Furthermore, these interacting proteins colocalize in the RPE. Cellular reconstitution of human interacting proteins shows that FATP1 markedly inhibits 11-cis Retinol production by acting on the production of all-trans retinyl esters and the isomerase activity of RPE65. The identification of this new visual cycle inhibitory component in RPE may contribute to further understanding of retinal pathogenesis.

Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes

Biochim Biophys Acta 1998 Oct 2;1394(1):16-22.PMID:9767084DOI:10.1016/s0005-2760(98)00078-2.

Our recent finding of the co-localization of 11-cis retinyl esters and 11-cis retinyl ester hydrolase (11-cis REH) activity in bovine retinal pigment epithelium (RPE) plasma membrane (PM) has led us to explore the possibility that the PM may provide 11-cis retinal for rhodopsin regeneration. In the RPE, visual chromophore is synthesized via a membrane associated 11-cis Retinol dehydrogenase (11-cis RD). Accordingly, bovine RPE membranes enriched with either endoplasmic reticulum (ER) or plasma membrane (PM) enzyme markers were prepared and assayed for visual cycle enzyme activities. Pronounced 11-cis RD activity was associated with both ER- and PM-enriched membrane fractions. In contrast, 11-cis REH activity was mostly recovered in PM-enriched fractions while LRAT activity was found only in ER-enriched membranes. The finding that both 11-cis Retinol and 11-cis retinal can be produced at the PM of the bovine RPE strongly suggests that 11-cis retinyl esters at this subcellular locale serve as a precursor of visual chromophore for pigment regeneration.

The retina visual cycle is driven by cis retinol oxidation in the outer segments of cones

Vis Neurosci 2017 Jan;34:E004.PMID:28359344DOI:10.1017/S0952523817000013.

Vertebrate rod and cone photoreceptors require continuous supply of chromophore for regenerating their visual pigments after photoactivation. Cones, which mediate our daytime vision, demand a particularly rapid supply of 11-cis retinal chromophore in order to maintain their function in bright light. An important contribution to this process is thought to be the chromophore precursor 11-cis Retinol, which is supplied to cones from Müller cells in the retina and subsequently oxidized to 11-cis retinal as part of the retina visual cycle. However, the molecular identity of the cis retinol oxidase in cones remains unclear. Here, as a first step in characterizing this enzymatic reaction, we sought to determine the subcellular localization of this activity in salamander red cones. We found that the onset of dark adaptation of isolated salamander red cones was substantially faster when exposing directly their outer vs. their inner segment to 9-cis retinol, an analogue of 11-cis Retinol. In contrast, this difference was not observed when treating the outer vs. inner segment with 9-cis retinal, a chromophore analogue which can directly support pigment regeneration. These results suggest, surprisingly, that the cis-retinol oxidation occurs in the outer segments of cone photoreceptors. Confirming this notion, pigment regeneration with exogenously added 9-cis retinol was directly observed in the truncated outer segments of cones, but not in rods. We conclude that the enzymatic machinery required for the oxidation of recycled cis retinol as part of the retina visual cycle is present in the outer segments of cones.

Structures important in NAD(P)(H) specificity for mammalian retinol and 11-Cis-retinol dehydrogenases

Biochem Biophys Res Commun 1996 Sep 4;226(1):118-27.PMID:8806601DOI:10.1006/bbrc.1996.1320.

Mammalian retinol and 11-cis Retinol dehydrogenases catalyze the formation of retinaldehyde from retinol and 11-cis retinaldehyde from 11-cis Retinol, respectively. Although their amino acid sequences are 54% identical, these enzymes have different cofactor specificities: rat retinol dehydrogenase uses NADP+, while cow 11-cis Retinol dehydrogenase uses NAD+. We used their close sequence similarity and the availability of 3D structures of their homologs to construct a 3D model of the two retinol dehydrogenases to investigate the determinants for cofactor specificity. The structure of rat retinol dehydrogenase shows that lysine-64 is important in stabilizing binding of 2'-phosphate on NADP+ in two ways: lysine's positively charged side chain has a coulombic attraction to the 2'-phosphate and partially compensates for the negative charge of aspartic acid-38. Cow 11-cis Retinol dehydrogenase has threonine-61 at the position homologous to lysine-64. Threonine-61 does not have a stabilizing coulombic interaction with NADP+, nor can threonine-61 counteract the repulsive interaction between NADP+ and aspartic acid-37 in 11-cis Retinol dehydrogenase. This suggests that aspartic acid-37 and threonine-61 are important in the specificity of 11-cis Retinol dehydrogenase for NAD+.

Hydrolysis of 11-cis- and all-trans-retinyl palmitate by retinal pigment epithelium microsomes

J Biol Chem 1992 May 15;267(14):9794-9.PMID:1577814doi

A partial characterization of the enzymatic hydrolysis of 11-cis- and all-trans-retinyl palmitate by bovine retinal pigment epithelium microsomes was carried out using a micro-radiometric method to quantitate liberated palmitic acid. Retinyl ester hydrolase (REH) activity was examined in the absence of detergent. Hydrolysis of 11-cis- and all-trans-retinyl palmitate was protein- and time-dependent. Optimal enzyme activity occurred at slightly alkaline pH (8-9). Apparent kinetic constants (Vmax and Km) for the 11-cis-REH were 2.1 nmol/min/mg protein and 66 microM, respectively. All-trans-REH demonstrated a lower maximum velocity of 0.3 nmol/min/mg protein and a slightly higher substrate affinity of 27 microM. Further characterization of 11-cis-retinyl palmitate hydrolysis involved monitoring formation of reaction products, 11-cis Retinol and palmitic acid, which were found to be released in essentially a 1:1 stoichiometry. Addition of all-trans retinyl bromoacetate, a known inhibitor of lecithin:retinol acyltransferase reduced both 11-cis and all-trans-REH activities but to significantly different degrees (50 and 76%, respectively). Although the microsomal preparation exhibited LRAT activity, acyl transfer was not readily reversible as labeled palmitic acid was not transferred to added acyl acceptor compounds. These findings suggest that hydrolysis of 11-cis-retinyl palmitate by bovine retinal pigment epithelium microsomes may occur at a catalytic site distinct from that for the all-trans isomer and that this hydrolysis is not representative of a reverse transesterification reaction.