Analytical Data
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Gene name
VKORC1
- Application
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Alternative Names
Vitamin K epoxide reductase complex subunit 1. EC:1.17.4.4. Vitamin K1 2.3-epoxide reductase subunit 1
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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
Q9BQB6
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Expression Region
1-163 aa
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AA Sequence
MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH
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Molecular Weight
44.6 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
VKORC1 (Vitamin K epoxide reductase complex subunit 1) is a critical enzyme involved in the vitamin K cycle, essential for the synthesis of various coagulation factors required for normal blood clotting. It catalyzes the reduction of vitamin K epoxide to its active form, thereby facilitating the carboxylation of glutamic acid residues in these proteins. Variations in the VKORC1 gene can significantly influence individual responses to anticoagulant medications, particularly warfarin, a commonly prescribed blood thinner. Understanding the structure and function of VKORC1 is vital for developing personalized anticoagulation therapies and improving patient outcomes. Recent advancements in recombinant protein technology have enabled the production of VKORC1 in heterologous systems, allowing researchers to study its biochemical properties in detail. By creating recombinant VKORC1, scientists aim to elucidate the enzyme's mechanism of action, characterize its interaction with vitamin K, and assess the impact of genetic variants on its functionality. This research not only enhances our knowledge of hemostasis but also has significant clinical implications for optimizing anticoagulant therapy in patients, reducing the risks of bleeding complications and improving therapeutic efficacy. Thus, VKORC1 recombinant protein studies hold crucial potential for both basic and translational research in hematology and pharmacogenomics.
