Analytical Data
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Gene name
DHRSX
- Application
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Alternative Names
CXorf11; Dehydrogenase/reductase (SDR family) X linked; Dehydrogenase/reductase SDR family member on chromosome X; DHRS5X; DHRS5Y; DHRSX; DHRSX_HUMAN; DHRSXY; DHRSY; RP11 325D5.2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N5I4
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Expression Region
1-330aa
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AA Sequence
MSPLSAARAALRVYAVGAAVILAQLLRRCRGGFLEPVFPPRPDRVAIVTGGTDGIGYSTAKHLARLGMHVIIAGNNDSKAKQVVSKIKEETLNDKVEFLYCDLASMTSIRQFVQKFKMKKIPLHVLINNAGVMMVPQRKTRDGFEEHFGLNYLGHFLLTNLLLDTLKESGSPGHSARVVTVSSATHYVAELNMDDLQSSACYSPHAAYAQSKLALVLFTYHLQRLLAAEGSHVTANVVDPGVVNTDLYKHVFWATRLAKKLLGWLLFKTPDEGAWTSIYAAVTPELEGVGGRYLYNEKETKSLHVTYNQKLQQQLWSKSCEMTGVLDVTL
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Molecular Weight
62.9 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
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Protein Description
The DHRSX gene, a member of the short-chain dehydrogenase/reductase (SDR) family, has attracted considerable attention in recent years due to its potential roles in various biological processes and disease mechanisms. Research indicates that DHRSX may be involved in important functions such as steroid metabolism and cellular responses to oxidative stress, both of which are critical in developmental and physiological contexts. Its expression pattern is notably enriched in reproductive tissues, hinting at a potential role in fertility and reproductive health. Furthermore, investigations into the enzyme's substrate specificity and coenzyme preference could unveil its physiological substrates and contribute to understanding its biological significance. Recent advances in molecular biology techniques have facilitated the functional characterization of DHRSX, making it possible to create recombinant proteins for in vitro studies. This is particularly important for elucidating the enzyme's catalytic mechanisms and regulatory pathways. Understanding the biochemical properties of DHRSX can ultimately provide insights into its contribution to reproductive biology and its potential involvement in pathophysiological conditions, such as hormonal dysregulation or fertility disorders. Hence, the study of DHRSX and its recombinant protein forms represents a promising avenue for research that could pave the way for novel therapeutic strategies targeting reproductive health and related disorders.
