Recombinant Human Retinol Dehydrogenase 12 (RDH12) Protein (His-SUMO)

Name: Recombinant Human Retinol Dehydrogenase 12 (RDH12) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10119P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Retinol Dehydrogenase 12 (RDH12) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q96NR8
Target Symbol	RDH12
Synonyms	All trans and 9 cis retinol dehydrogenase; All-trans and 9-cis retinol dehydrogenase; LCA 3; LCA13; LCA3; RDH 12; RDH12; RDH12_HUMAN; Retinol dehydrogenase 12 (all trans/9 cis/11 cis); Retinol dehydrogenase 12 all trans and 9 cis; Retinol dehydrogenase 12; RP53; SDR7C2; Short chain dehydrogenase/reductase family 7C member 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MLVTLGLLTSFFSFLYMVAPSIRKFFAGGVCRTNVQLPGKVVVITGANTGIGKETARELASRGARVYIACRDVLKGESAASEIRVDTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLHILINNAGVMMCPYSKTADGFETHLGVNHLGHFLLTYLLLERLKVSAPARVVNVSSVAHHIGKIPFHDLQSEKRYSRGFAYCHSKLANVLFTRELAKRLQGTGVTTYAVHPGVVRSELVRHSSLLCLLWRLFSPFVKTAREGAQTSLHCALAEGLEPLSGKYFSDCKRTWVSPRARNNKTAERLWNVSCELLGIRWE
Expression Range	1-316aa
Protein Length	Full Length
Mol. Weight	51.1kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity towards 13-cis-retinol. Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal. May play an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation. Has no dehydrogenase activity towards steroids.
Subcellular Location	Endoplasmic reticulum membrane.
Protein Families	Short-chain dehydrogenases/reductases (SDR) family
Database References	HGNC: 19977 OMIM: 608830 KEGG: hsa:145226 STRING: 9606.ENSP00000267502 UniGene: PMID: 28471114 Peripapillary sparing is a novel phenotypic feature of RDH12-associated Leber congenital amaurosis. PMID: 28513254 The mutation detection of RDH12 in this study also implies that whole exome sequencing is a useful method for detection of potential mutations in small families with atypical clinical manifestations of genetic disease. PMID: 26848971 We report 4 children from 3 consanguineous families with bilateral elevation deficiency in the context of retinal dystrophy. All were found to harbor recessive mutations in retinal dehydrogenase 12 (RDH12). PMID: 26691045 Mutations in the AIPL1 and RDH12 genes associated with leber congenital amaurosis in two Turkish families. PMID: 25148430 Here we demonstrate that microtubule-associated protein 1 light chain 3A (LC3A), a marker of autophagy, is related to hypoxia and poor prognosis in clear cell ovarian cancer. PMID: 22926683 The three patients with Leber congenital amaurosis/early-onset retinal dystrophy had a progressive decrease of their vision with the formation of a posterior staphyloma. PMID: 24752437 Two novel missense mutations in the RDH12 gene are associated with retinitis pigmentosa. PMID: 23900199 Seventeen novel mutations in the RDH12 gene were identified that accounted for approximately 7% of disease in a cohort of patients diagnosed with Leber congenital amaurosis and early-onset retinal dystrophy. PMID: 22065924 LCA has been associated with sequence variations of 14 different genes; in approximately 30% of all cases pathogenic mutations remain to be determined. PMID: 20736127 The retina RDH12 reduces 4-HNE to a nontoxic alcohol, protecting cellular macromolecules against oxidative modification and protecting photoreceptors from light-induced apoptosis. PMID: 19686838 Results suggest that the accelerated degradation of RDH12 mutants by the ubiquitin-proteasome system contributes to the pathophysiology and phenotypic variability associated with mutations in the RDH12 gene. PMID: 20006610 Our studies show that RDH12 is associated with retinal dystrophy and encodes an enzyme with a unique, nonredundant role in the photoreceptor cells. PMID: 15258582 All patients harboring RDH12 mutations had a severe yet progressive rod-cone dystrophy with severe macular atrophy but no or mild hyperopia. PMID: 15322982 In most tissues RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, in cells undergoing oxidative stress, such as photoreceptors, RDH12 might also play a role in detoxification of lipid peroxidation products. PMID: 15865448 The results demand critical consideration of the human disease mechanism and the therapeutic approach in patients with mutations in the putative visual cycle gene RDH12. PMID: 17197551 Ophthalmic findings in persons with RDH12 mutations suggest that RDH12 loss-of-function results in a characteristic form of early and progressive rod-cone degeneration PMID: 17389517 Human type 12 RDH reduces dihydrotestosterone to androstanediol, and is thus involved in steroid metabolism. PMID: 17512723 in patients with Leber congenital amaurosis, autosomal recessive retinitis pigmentosa, and autosomal dominant/recessive cone-rod dystrophies six different variants of RDH12 were observed of which three variants were novel PMID: 17512964 The demonstration that mutations in a gene previously associated with recessive Leber congenital amaurosis can also cause dominant RP illustrates the wide phenotypic variability of retinal degeneration genes. PMID: 18779497 The RDH12-associated phenotype is not homogeneous, the position and nature of the mutations clearly influence the pathologic expression of this disease. PMID: 19011012

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.