Analytical Data
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Gene name
TRIM73
- Application
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Alternative Names
TRIM73; TRIM50B; Tripartite motif-containing Protein 73; Tripartite motif-containing Protein 50B
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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
Q86UV7
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Expression Region
1-250 aa
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AA Sequence
MAWQVSLLEL EDRLQCPICL 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
Related Products
Protein Description
TRIM73, a member of the TRIM (tripartite motif-containing) protein family, has garnered significant attention in recent years due to its potential roles in various biological processes and disease mechanisms. This protein is characterized by a distinctive tripartite structure comprised of RING, B-box, and coiled-coil domains, which are critical for its function in ubiquitination and protein stability regulation. Research has indicated that TRIM73 may be involved in cellular processes such as immune responses, cell proliferation, and apoptosis, suggesting its significance in maintaining cellular homeostasis. Furthermore, aberrant expression or dysregulation of TRIM73 has been implicated in several pathological conditions, including cancer progression and autoimmune diseases. Investigations into the functional mechanisms of TRIM73 have led to its exploration as a potential therapeutic target, prompting the development of recombinant TRIM73 proteins for various applications. These recombinant proteins are instrumental in elucidating TRIM73's molecular interactions and pathways, advancing our understanding of its role in health and disease. Overall, the study of TRIM73 and its recombinant forms represents a promising frontier in molecular biology, offering insights into targeted therapies and novel diagnostic tools for cancer and other disorders where TRIM73 is a contributing factor.
