Analytical Data
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Gene name
RDH11
- Application
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Alternative Names
RDH11；ARSDR1；PSDR1；SDR7C1；Retinol dehydrogenase 11
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TC12
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Expression Region
22-318aa
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AA Sequence
PQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID
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Molecular Weight
49.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
RDH11, a member of the short-chain dehydrogenase/reductase (SDR) superfamily, plays a crucial role in cellular metabolism and the regulation of retinoic acid levels, which are essential for various developmental processes. Its involvement in the oxidation-reduction reactions of retinol and other potential substrates has sparked interest in understanding its biological functions. Recent studies indicate that RDH11 may contribute to the metabolism of retinoids and other lipid-soluble metabolites, influencing cellular differentiation and proliferation. Additionally, alterations in RDH11 expression have been linked to several pathological conditions, including cancer and neurodegenerative disorders. Despite its significance, the precise mechanisms by which RDH11 exerts its effects in these contexts remain poorly characterized. Consequently, research on RDH11 recombinant proteins aims to elucidate its biochemical properties, explore its interactions with various substrates, and assess its potential as a therapeutic target. The generation of functional RDH11 recombinant proteins facilitates in vitro studies to investigate its enzymatic activity, substrate specificity, and regulatory mechanisms. Understanding these aspects might provide new insights into its role in health and disease, paving the way for the development of novel therapeutic strategies targeting RDH11-related pathways.
