Analytical Data
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Gene name
TRIM7
- Application
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Alternative Names
(Glycogenin-interacting protein)(RING finger protein 90)(Tripartite motif-containing protein 7)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9C029
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Expression Region
1-511aa
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Molecular Weight
64.1 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
TRIM7 (Tripartite Motif-containing Protein 7) is a member of the TRIM protein family, which plays critical roles in various cellular processes, including immune response, cell signaling, and apoptosis. Recent studies have highlighted TRIM7's involvement in the modulation of inflammatory pathways and its potential role as an E3 ubiquitin ligase. This suggests that TRIM7 may influence the stability of target proteins, thereby regulating key biological functions. The study of TRIM7 recombinant proteins is particularly important for understanding its functional mechanisms and potential therapeutic applications. Researchers have been focusing on characterizing TRIM7 through recombinant expression systems, enabling them to produce large quantities of the protein for biochemical and structural analyses. This has allowed for the exploration of TRIM7's interactions with other cellular partners and its role in disease pathogenesis, such as in cancer and viral infections. By examining the structure-function relationship of TRIM7, scientists aim to elucidate its contributions to cellular homeostasis and its potential as a target for novel therapeutic strategies. The ongoing research on TRIM7 recombinant proteins continues to reveal insights into the complex regulatory networks involving this protein, paving the way for future studies that may harness TRIM7's properties for therapeutic advancements.
