Analytical Data
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Gene name
TRIM3
- Application
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Alternative Names
BERP; HAC1; RNF22; RNF97; Ring Finger Protein 22; RING finger protein 97; Brain Expressed Ring Finger; Tripartite Motif Protein TRIM3
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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
O75382
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Expression Region
Ala2~Arg152
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Molecular Weight
20kDa
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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
TRIM3, a member of the tripartite motif (TRIM) family of proteins, has garnered significant attention in recent years due to its potential roles in various biological processes and diseases, particularly in cancer and neurodegenerative disorders. This protein possesses an E3 ubiquitin ligase activity, which allows it to regulate protein degradation and signaling pathways by ubiquitination. Research has shown that TRIM3 can influence cell proliferation, apoptosis, and immune responses, suggesting its involvement in tumorigenesis and the immune system. Moreover, studies indicate that dysregulation of TRIM3 expression may contribute to the pathogenesis of certain cancers and neurodegenerative diseases, such as Alzheimer's and Parkinson's. The exploration of TRIM3 as a therapeutic target is gaining momentum, with efforts directed towards understanding its molecular mechanisms and interactions with other cellular components. Using recombinant TRIM3 proteins for functional assays and structural studies could provide insights into the protein's role in vivo and lead to novel treatment strategies aimed at modulating its activity in disease contexts. Understanding TRIM3's function and regulatory mechanisms may ultimately illuminate new avenues for therapeutic intervention and enhances our understanding of cellular homeostasis in health and disease.
