Analytical Data
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Gene name
HIV1
- Application
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Alternative Names
HIV1；AIP1；ALIX；KIAA1375；Programmed cell death 6-interacting Protein
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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
P03367
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Expression Region
501-599aa
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AA Sequence
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGI GGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF
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Molecular Weight
11 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
Research on HIV-1 recombinant proteins has gained significant attention due to the urgent need for effective prevention and therapeutic strategies against HIV/AIDS. HIV-1, the most prevalent strain responsible for the global epidemic, has a complex structure and a high mutation rate, making vaccine development particularly challenging. Recombinant proteins, which are artificially produced proteins derived from the HIV-1 genome, are essential for various applications, including vaccine development, diagnostic assays, and studying viral mechanisms. These proteins can stimulate the immune response, allowing researchers to identify potential epitopes for vaccine candidates. Moreover, understanding the structure and function of HIV-1 proteins, such as env, gag, and pol, helps in elucidating the virus's lifecycle and pathogenicity. With advancements in biotechnology, including synthetic biology and protein engineering, the production of these recombinant proteins has become more efficient, supporting large-scale studies. This research not only provides insights into the immune response to HIV-1 but also aids in the design of novel antiviral therapies. As global efforts to combat HIV/AIDS continue, the exploration of HIV-1 recombinant proteins remains crucial for developing strategies that can ultimately lead to the eradication of the virus and a better quality of life for those affected.
