Analytical Data
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Gene name
Veph1
- Application
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Alternative Names
Protein melted homolog (Veph)
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A1A535
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Expression Region
660-833aa
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Molecular Weight
27.7 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
Veph1, a novel protein derived from the viral envelope protein of certain pathogens, has garnered significant interest in research due to its potential roles in immune response modulation and pathogen interaction. The study of Veph1 is crucial because it may provide insights into the mechanisms of viral entry into host cells, thereby offering a deeper understanding of viral pathogenesis. Moreover, given its potential to influence host immune responses, Veph1 could serve as a key target for the development of therapeutic strategies aimed at enhancing immune defense or creating more effective vaccines. As researchers continue to investigate the structural and functional aspects of Veph1, including its interaction with host cell receptors and subsequent intracellular signaling pathways, there is increasing hope that these findings could lead to breakthroughs in managing viral infections. Understanding the dynamics of Veph1 not only holds promise for virology and immunology but could also inform broader applications in biotechnology and drug design. Consequently, ongoing research into Veph1 reaffirms its significance in advancing our comprehension of viral biology and enhancing public health interventions against viral diseases.
