Analytical Data
-
Gene name
RDH13
- Application
-
Alternative Names
PSEC0082; RDH13; RDH13_HUMAN; Retinol dehydrogenase 13 (all trans and 9 cis); Retinol dehydrogenase 13 (all trans/9 cis); Retinol dehydrogenase 13; UNQ736/PRO1430
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NBN7
-
Expression Region
1-331 aa
-
AA Sequence
MSRYLLPLSA LGTVAGAAVL LKDYVTGGAC PSKATIPGKT VIVTGANTGI GKQTALELAR RGGNIILACR DMEKCEAAAK DIRGETLNHH VNARHLDLAS LKSIREFAAK IIEEEERVDI LINNAGVMRC PHWTTEDGFE MQFGVNHLGH FLLTNLLLDK LKASAPSRII NLSSLAHVAG HIDFDDLNWQ TRKYNTKAAY CQSKLAIVLF TKELSRRLQG SGVTVNALHP GVARTELGRH TGIHGSTFSS TTLGPIFWLL VKSPELAAQP STYLAVAEEL ADVSGKYFDG LKQKAPAPEA EDEEVARRLW AESARLVGLE APSVREQPLP R
-
Molecular Weight
35.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
RDH13 (retinol dehydrogenase 13) is a member of the aldo-keto reductase superfamily and plays a crucial role in the metabolism of retinoids, which are essential for vision, embryonic development, and cellular differentiation. This enzyme catalyzes the reduction of retinaldehyde to retinol, contributing to the maintenance of retinoid homeostasis in tissues. Dysregulation of RDH13 has been implicated in various diseases, including cancer and metabolic disorders, highlighting its potential as a therapeutic target. Recent studies have focused on the structure-function relationship of RDH13, emphasizing the importance of its active site and substrate specificity. Additionally, the expression patterns of RDH13 in different tissues suggest its functional diversity and regulatory mechanisms. Research on recombinant RDH13 proteins aims to elucidate its enzymatic activity, regulatory pathways, and interaction with retinoid substrates. Understanding these aspects could provide insights into the role of RDH13 in health and disease, paving the way for novel strategies in therapeutic interventions. As such, the production and characterization of RDH13 recombinant proteins are critical steps in exploring this enzyme's potential in basic and applied biomedical research.











