Analytical Data
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Gene name
int
- Application
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Species
Escherichia phage lambda
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03700
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Expression Region
1-356aa
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Molecular Weight
46.3 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
The study of Int protein, a critical component of the integrase enzyme, is rooted in its role in the lifecycle of retroviruses and transposable elements. Integrases catalyze the integration of viral DNA into the host genome, a crucial step for viral replication and persistence. Research into Int proteins has gained momentum due to their significance in understanding viral pathogenesis and the development of targeted antiviral therapies. Furthermore, Int proteins have emerged as key players in the field of genetic engineering and biotechnology, as their unique ability to mediate precise DNA integration offers promising avenues for gene therapy applications. Investigations into the structural and functional properties of Int proteins have revealed insights into their mechanism of action, enabling rational design of integrase inhibitors to combat retroviral infections, such as HIV. Additionally, the evolutionary conservation of these proteins suggests potential applications in synthetic biology and the advancement of gene-editing technologies. Understanding the intricacies of Int protein interactions and their regulatory networks remains a vibrant area of research, with implications not only for virology and medicine but also for advancing biotechnological innovations. As researchers continue to unravel the complexities of Int proteins, the knowledge gained may lead to groundbreaking strategies for controlling viral diseases and enhancing genetic manipulation techniques for therapeutic purposes.
