Analytical Data
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基因名
TRIM10
- Application
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别名
TRIM10; RFB30; RNF9; Tripartite motif-containing Protein 10; B30-RING finger Protein; RING finger Protein 9
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UDY6
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表达区间
1-481 aa
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氨基酸序列
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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分子量
55.0 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
