Analytical Data
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Gene name
VIP
- Application
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Alternative Names
PHM27; Intestinal peptide PHV-42; Peptide histidine valine 42; Peptide histidine methioninamide 27
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Species
Human
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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
P01282
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Expression Region
Tyr29~Pro165
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Molecular Weight
15/16kDa
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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 study of VIP (vasoactive intestinal peptide) recombinant proteins has gained significant attention in recent years due to their multifaceted roles in physiological processes and potential therapeutic applications. VIP is a neuropeptide originally identified for its role in vasodilation, but research has revealed its involvement in various biological functions, including modulation of immune responses, regulation of circadian rhythms, and neuroprotection. The ability to recombine VIP into novel proteins enhances understanding of its structure-function relationships, facilitating the design of targeted therapies for conditions such as inflammatory disorders, neurodegenerative diseases, and gastrointestinal issues. Advances in recombinant DNA technology allow for the production of structurally modified VIP proteins with improved stability, potency, and specificity. These studies not only aim to elucidate the mechanisms underlying VIP’s diverse effects but also explore its potential as a biomarker and therapeutic agent. Given the rising incidence of diseases linked to dysregulation of peptide signaling pathways, ongoing research into VIP recombinant proteins holds promise for developing innovative treatment strategies. Furthermore, the exploration of VIP as an influential player in neuro-immunoendocrine regulation underscores its relevance in comprehensive health research, potentially leading to breakthroughs in personalized medicine and broader applications in biotechnology.
