Analytical Data
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Gene name
VNN3
- Application
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Alternative Names
VNN3；Vascular non-inflammatory molecule 3
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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
Q9NY84-2
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Expression Region
175-274aa
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AA Sequence
ARYHKYNLFAPEIQFDFPKDSELVTFDTPFGKFGIFTCFDIFSHDPAVVV VDEFQLTAFSTPQHGTTRCPSSRLFPSIQHGPRPWESIYLLQIPTTPACT
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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
VNN3 (vanin-3) is a member of the family of pantetheinases, enzymes that play a crucial role in the metabolism of coenzyme A and the regulation of cellular redox state. Research into VNN3 has gained momentum due to its involvement in various physiological processes and pathophysiological conditions, including inflammation, oxidative stress, and cancer. It is primarily expressed in tissues such as the brain, heart, and immune cells, indicating its importance in both neurological functions and immune response. Recent studies have suggested that VNN3 may act as a modulator of inflammation, possibly influencing the development of chronic diseases. Furthermore, the exploration of VNN3 as a therapeutic target has been fueled by the observation that modulating its activity can alter disease outcomes in models of autoimmune disorders and tumorigenesis. The recombinant expression of VNN3 protein facilitates a better understanding of its structure-function relationships, allowing researchers to investigate potential inhibitors or activators that could serve as novel therapeutic agents. As such, the study of VNN3 not only contributes to the fundamental understanding of enzymatic roles in cellular function but also opens new avenues for therapeutic intervention in diseases where inflammation and oxidative stress play pivotal roles. Overall, VNN3 represents a promising candidate for future research aimed at elucidating its biological functions and therapeutic potential in various clinical applications.
