Analytical Data
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Gene name
VNN1/Vanin-1
- Application
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Alternative Names
Pantetheinase; Pantetheine hydrolase; Tiff66; Vascular non-inflammatory molecule 1
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Species
Bovine
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q58CQ9
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Expression Region
Leu216~Gly469
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Molecular Weight
29kDa
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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
VNN1, also known as Vanin-1, is a member of the Vanin family of proteins and is primarily expressed in various tissues, including the kidney, liver, and intestine. It serves a crucial role in the metabolism of the antioxidant glutathione and is involved in the modulation of immune responses as well as inflammatory processes. Research has indicated that VNN1 plays a significant role in the regulation of oxidative stress, with implications for various pathological conditions, including cardiovascular diseases, cancer, and neurodegenerative disorders. Given its pivotal functions, there is increasing interest in recombinant VNN1 protein as a therapeutic target. Studies focus on its structure, enzymatic activity, and potential interactions with other cellular mechanisms. Understanding the molecular characteristics and biological functions of VNN1 can facilitate the development of novel strategies for disease intervention, particularly in conditions characterized by oxidative imbalance. Furthermore, recombinant VNN1 protein offers opportunities for exploring its application in drug development and therapeutic interventions, enabling researchers to investigate how modulating its activity could benefit patient outcomes in diseases where oxidative stress is a contributing factor. Thus, the ongoing exploration of VNN1/Vanin-1 serves as a promising avenue for advancing biomedical research and enhancing our comprehension of its multifaceted roles in health and disease.
