Analytical Data
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Gene name
TRIM74
- Application
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Alternative Names
TRIM74; TRIM50C; Tripartite motif-containing Protein 74; Tripartite motif-containing Protein 50C
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86UV6
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Expression Region
1-250 aa
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AA Sequence
MAWQVSLLEL EDWLQCPICL EVFKESLMLQ CGHSYCKGCL VSLSYHLDTK VRCPMCWQVV DGSSSLPNVS LAWVIEALRL PGDPEPKVCV HHRNPLSLFC EKDQELICGL CGLLGSHQHH PVTPVSTVCS RMKEELAALF SELKQEQKKV DELIAKLVKN RTRIVNESDV FSWVIRREFQ ELRHPVDEEK ARCLEGIGGH TRGLVASLDM QLEQAQGTRE RLAQAECVLE QFGNEDHHEF IWKFHSMASR
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Molecular Weight
28.5 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
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Protein Description
TRIM74 is a member of the tripartite motif (TRIM) protein family, characterized by their RING finger, B-box, and coiled-coil domains, which play crucial roles in various biological processes, including immune response, cell differentiation, and tumor suppression. Recent studies have highlighted TRIM74's potential as a significant player in regulating cellular functions related to cancer and viral infections. The protein is thought to modulate signal transduction pathways and influence the stability of other proteins through its E3 ubiquitin ligase activity. Given its involvement in the innate immune response, TRIM74 has garnered attention for its potential therapeutic applications against cancers and viral diseases. The exploration of TRIM74 as a recombinant protein has enabled detailed functional analyses, offering insights into its role in protein-protein interactions and post-translational modifications. Research often focuses on purifying TRIM74 and characterizing its biochemical properties, as well as its impact on cellular mechanisms. The findings suggest that manipulating TRIM74 may provide novel strategies for cancer treatment and enhance our understanding of viral pathogenesis. Overall, the ongoing investigation of TRIM74 and its recombinant forms marks a significant advancement in the field of molecular biology and presents exciting opportunities for future therapeutic interventions.
