Analytical Data
-
Gene name
TRIM5
- Application
-
Alternative Names
TRIM5α; TRIM5alpha; TRIM5-alpha; RNF88; RING finger protein 88
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9C035
-
Expression Region
Ala2~Thr261
-
Molecular Weight
36kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
TRIM5 is a member of the tripartite motif (TRIM) family of proteins, which play crucial roles in various cellular processes, including immune response and protein degradation. One of the most fascinating aspects of TRIM5 is its role in innate immunity, particularly in recognizing and inhibiting retroviral infections, such as those caused by HIV. The protein contains a RING domain, B-box, and coiled-coil region, which contribute to its function as an antiviral factor. The study of TRIM5 has gained significant attention due to its ability to bind directly to the capsid of incoming retroviruses, leading to their destabilization and preventing successful infection. Interestingly, different primate species exhibit variations in TRIM5 alleles, leading to differences in susceptibility to various retroviruses, providing valuable insights into evolutionary biology and host-pathogen interactions. Research on TRIM5 recombinant proteins aims to elucidate their mechanisms of action and potential therapeutic applications, such as developing antiviral strategies or enhancing immune responses against retroviral infections. Additionally, TRIM5 has been implicated in modulating several cellular pathways, including autophagy and inflammation, thereby highlighting its multifunctional nature. Overall, the exploration of TRIM5 recombinant proteins is crucial not only for understanding the intricacies of viral recognition and resistance but also for paving the way toward novel biomedical interventions in the fight against viral diseases.
