Analytical Data
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Gene name
DHCR7
- Application
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Alternative Names
DHCR7；D7SR；7-dehydrocholesterol reductase
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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
Q9UBM7
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Expression Region
1-475aa
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AA Sequence
MAAKLQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFA PFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLY TLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQA WLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGY FFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTL INLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHD HFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYI FRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFW GVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHR CASKYGRDWERYTAAVPYRLLPGIF
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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
DHCR7 (7-dehydrocholesterol reductase) is an essential enzyme involved in the cholesterol biosynthesis pathway, specifically catalyzing the conversion of 7-dehydrocholesterol to cholesterol. Mutations in the DHCR7 gene are linked to Smith-Lemli-Opitz syndrome (SLOS), a genetic disorder characterized by a range of developmental and physical abnormalities due to impaired cholesterol synthesis. The investigation of DHCR7 and its recombinant protein has gained prominence due to its vital role in cellular membrane integrity and signaling, as well as its implications in developmental biology and disease mechanisms. Researchers are particularly interested in the structure-function relationship of the DHCR7 protein, as understanding its dynamics may provide insights into therapeutic strategies for conditions stemming from cholesterol biosynthesis defects. Furthermore, recombinant DHCR7 can serve as a valuable tool in drug discovery and development, aiding in the creation of compounds that can either mimic its activity or regulate its function. By elucidating the enzymatic activity and regulatory mechanisms of DHCR7 through in vitro studies and structural analysis, scientists hope to uncover potential intervention points for treating SLOS and related cholesterol metabolism disorders. Overall, the study of DHCR7 recombinant protein stands at the intersection of basic biochemistry and clinical application, highlighting the enzyme's significance in both healthy physiology and disease pathology.
