Analytical Data
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Gene name
gag
- Application
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Alternative Names
gag；Gag polyProtein
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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
Q9UL42
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Expression Region
2-361aa
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AA Sequence
ALALLEDWCRIMSVDEQKSLMVTGIPADFEEAEIQEVLQETLKSLGRYRLLGKIFRKQENANAVLLELLEDTDVSAIPSEVQGKGGVWKVIFKTPNQDTEFLERLNLFLEKEGQTVSGMFRALGQEGVSPATVPCISPELLAHLLGQAMAHAPQPLLPMRYRKLRVFSGSAVPAPEEESFEVWLEQATEIVKEWPVTEAEKKRWLAESLRGPALDLMHIVQADNPSISVEECLEAFKQVFGSLESRRTAQVRYLKTYQEEGEKVSAYVLRLETLLRRAVEKRAIPRRIADQVRLEQVMAGATLNQMLWCRLRELKDQGPPPSFLELMKVIREEEEEEASFENESIEEPEERDGYGRWNHE
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Molecular Weight
57.1 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
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Protein Description
Gag proteins, primarily derived from retroviruses, play a crucial role in the viral life cycle, particularly during the assembly and budding processes of new virions. Research on Gag proteins focuses on their structural and functional characteristics, as these proteins are essential for encapsulating viral RNA and facilitating the formation of viral particles. The understanding of Gag protein interactions with host cell machinery and other viral elements has significant implications for the development of antiviral therapies and vaccines. Moreover, Gag proteins are being explored in the context of gene therapy and vaccine delivery systems, as their ability to self-assemble and package genetic material presents innovative avenues for therapeutic applications. In recent years, advancements in molecular biology techniques, such as CRISPR and high-throughput sequencing, have enabled researchers to elucidate the intricate mechanisms behind Gag protein functions and their interactions within the cellular environment. This ongoing research not only enhances our understanding of retroviral biology but also opens doors for the development of novel strategies to combat viral infections and harness Gag proteins for beneficial uses in biotechnology and medicine.
