Analytical Data
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Gene name
gag-pol
- Application
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Alternative Names
(Pr180gag-pol)(pp12)(Capsid protein p30)(CA)(NC-pol)(p14)(p46)
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Species
Moloney murine leukemia virus
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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
P03355
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Expression Region
660-1330aa
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Molecular Weight
82.1 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
Gag-pol fusion proteins are critical components in the life cycle of retroviruses, particularly HIV, where they play significant roles in viral assembly and replication. These proteins are derived from the viral polyprotein precursor, Gag-Pol, which is subsequently cleaved by viral proteases into distinct functional domains. The gag portion is primarily responsible for forming the viral core structure, while pol encompasses essential enzymatic functions, including reverse transcriptase, integrase, and protease activities. Research on Gag-Pol proteins has gained momentum due to their pivotal roles in viral pathogenesis and potential as therapeutic targets. Understanding the structural and functional properties of these proteins could pave the way for novel antiviral strategies, including the design of inhibitors that disrupt their function. Additionally, Gag-Pol proteins are utilized in various biotechnological applications, such as the production of lentiviral vectors for gene therapy, which harness their ability to package and deliver genetic material into host cells. Consequently, ongoing studies aim to elucidate the molecular mechanisms governing Gag-Pol interactions and their dynamics during the viral life cycle, ultimately contributing to the development of effective interventions against retroviral infections.
