Analytical Data
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Gene name
TRIM10
- Application
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Alternative Names
TRIM10; RFB30; RNF9; Tripartite motif-containing Protein 10; B30-RING finger Protein; RING finger Protein 9
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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
Q9UDY6
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Expression Region
1-481 aa
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AA Sequence
MASAASVTSL ADEVNCPICQ GTLREPVTID CGHNFCRACL TRYCEIPGPD LEESPTCPLC KEPFRPGSFR PNWQLANVVE NIERLQLVST LGLGEEDVCQ EHGEKIYFFC EDDEMQLCVV CREAGEHATH TMRFLEDAAA PYREQIHKCL KCLRKEREEI QEIQSRENKR MQVLLTQVST KRQQVISEFA HLRKFLEEQQ SILLAQLESQ DGDILRQRDE FDLLVAGEIC RFSALIEELE EKNERPAREL LTDIRSTLIR CETRKCRKPV AVSPELGQRI RDFPQQALPL QREMKMFLEK LCFELDYEPA HISLDPQTSH PKLLLSEDHQ RAQFSYKWQN SPDNPQRFDR ATCVLAHTGI TGGRHTWVVS IDLAHGGSCT VGVVSEDVQR KGELRLRPEE GVWAVRLAWG FVSALGSFPT RLTLKEQPRQ VRVSLDYEVG WVTFTNAVTR EPIYTFTASF TRKVIPFFGL WGRGSSFSLS S
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Molecular Weight
55.0 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
TRIM10, a member of the tripartite motif (TRIM) protein family, has garnered interest in the field of molecular and cellular biology due to its potential roles in various physiological and pathological processes. Studies have shown that TRIM proteins are involved in diverse functions, including immune response regulation, cell differentiation, and oncogenesis. Specifically, TRIM10 has been implicated in the modulation of immune responses and the restriction of viral infections, showcasing its significance in infectious disease contexts. Additionally, aberrations in TRIM10 expression levels have been associated with several cancers, indicating its potential as a biomarker or therapeutic target. The reorganization of TRIM10 into a recombinant protein format facilitates in-depth investigations into its structure-function relationships, signaling pathways, and interactions with other cellular components. By employing techniques such as protein purification and functional assays, researchers aim to elucidate the molecular mechanisms underlying TRIM10's actions. Understanding TRIM10's role in cellular processes may provide insights into new therapeutic strategies for diseases associated with its dysregulation, especially in areas like cancer immunotherapy and viral infections. Thus, the study of TRIM10 recombinant protein not only enhances our understanding of this specific protein but also broadens the scope of TRIM proteins as critical players in health and disease.
