Analytical Data
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Gene name
TRIM11
- Application
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Alternative Names
Protein BIA1RING finger protein 92Tripartite motif-containing protein 11
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96F44
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Expression Region
267-468aa
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Molecular Weight
38.5 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
TRIM11, a member of the tripartite motif (TRIM) protein family, plays a crucial role in various cellular processes, including immune response, cell differentiation, and apoptosis. This protein features a RING-type zinc finger, B-box, and coiled-coil domains, which are essential for its E3 ubiquitin ligase activity. Recent studies have highlighted TRIM11's involvement in the regulation of several signaling pathways, particularly in the context of viral infections and cancer progression. It has been identified as an important factor in the ubiquitination of target proteins, thereby influencing their stability and activity. Notably, TRIM11 has been implicated in the modulation of the antiviral response, as it can enhance or inhibit the replication of certain viruses, suggesting a double-edged role in host-pathogen interactions. Moreover, aberrant expression of TRIM11 has been associated with various malignancies, making it a potential biomarker for cancer diagnosis and prognosis. Research into TRIM11's structure and function, as well as its role in disease mechanisms, is ongoing, with the aim of elucidating its therapeutic potential. Understanding TRIM11's intricate functions and interactions within cellular networks could pave the way for developing novel strategies to target its activity in diseases where it plays a critical role.
