Analytical Data
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Gene name
TRIM5
- Application
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Alternative Names
TRIM5α; TRIM5alpha; TRIM5-alpha; RNF88; RING finger protein 88
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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 90% as determined by SDS-PAGE.
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Uniprot
Q9C035
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Expression Region
Ala2~Thr261
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Molecular Weight
36kDa
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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
TRIM5 is a member of the tripartite motif (TRIM) family of proteins, known for its role in the innate immune response against retroviruses. The interest in TRIM5 research has escalated particularly due to its unique ability to recognize and restrict various retroviruses, including HIV-1, which poses significant challenges to global health. TRIM5 functions as a restriction factor by binding to the capsid of the incoming viral particles, leading to their recognition and subsequent degradation by the cellular proteasome. Understanding the mechanisms of TRIM5's antiviral activity is critical for the development of novel therapeutic strategies against retroviral infections. Additionally, variations in TRIM5 alleles among different primate species provide insights into the evolutionary pressures exerted by retroviruses, showcasing a fascinating interplay between host defense mechanisms and viral evasion strategies. Recent studies have also explored the potential of engineering TRIM5 proteins to enhance their antiviral efficacy, aiming to create new avenues for gene therapy and vaccine development. Thus, ongoing research into TRIM5 not only enriches our understanding of host-pathogen interactions but also holds promise for innovative approaches to combat retroviral diseases.
