Analytical Data
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Gene name
VC
- Application
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Alternative Names
VC；Unconventional myosin-Vc
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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
Q9NQX4
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Expression Region
全长
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AA Sequence
full
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Molecular Weight
202. 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
The research on VC (Vitamin C) recombinant proteins stems from the increasing interest in the therapeutic potential of vitamin C, particularly in oncology and immunology. Vitamin C, or ascorbic acid, is known for its essential role in various biological functions, including antioxidant activity and collagen synthesis. However, its application in clinical settings has been limited by challenges related to stability, bioavailability, and effective delivery systems. The advent of recombinant DNA technology has opened new avenues for producing VC in more stable and bioactive forms. Researchers aim to express VC as a recombinant protein using various host organisms, enabling better production scalability and enhanced biological activity. This approach not only facilitates the study of vitamin C's mechanisms but also aims to overcome the limitations of traditional supplementation methods. Additionally, the exploration of VC recombinant proteins is timely, as there is a growing body of evidence suggesting that vitamin C can enhance the efficacy of certain cancer therapies and bolster immune responses. Thus, the focus on VC recombinant protein research is driven by its potential to offer new therapeutic strategies in modern medicine, aimed at improving patient outcomes and exploring vitamin C's multifaceted roles in health and disease.
