Analytical Data
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基因名
TRIM14
- Application
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别名
5830400N10Rik ; KIAA0129; pub; TRI14_HUMAN; TRIM14; tripartite motif Protein 14; tripartite motif Protein TRIM14; tripartite motif-containing 14; Tripartite motif-containing Protein 14
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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
Q14142
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表达区间
1-442 aa
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氨基酸序列
MAGAATGSRT PGRSELVEGC GWRCPEHGDR VAELFCRRCR RCVCALCPVL GAHRGHPVGL ALEAAVHVQK LSQECLKQLA IKKQQHIDNI TQIEDATEKL KANAESSKTW LKGKFTELRL LLDEEEALAK KFIDKNTQLT LQVYREQADS CREQLDIMND LSNRVWSISQ EPDPVQRLQA YTATEQEMQQ QMSLGELCHP VPLSFEPVKS FFKGLVEAVE STLQTPLDIR LKESINCQLS DPSSTKPGTL LKTSPSPERS LLLKYARTPT LDPDTMHARL RLSADRLTVR CGLLGSLGPV PVLRFDALWQ VLARDCFATG RHYWEVDVQE AGAGWWVGAA YASLRRRGAS AAARLGCNRQ SWCLKRYDLE YWAFHDGQRS RLRPRDDLDR LGVFLDYEAG VLAFYDVTGG MSHLHTFRAT FQEPLYPALR LWEGAISIPR LP
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分子量
49.7 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
TRIM14, a member of the tripartite motif (TRIM) family of proteins, has garnered significant attention in recent years due to its implications in various biological processes, including immune response, cell proliferation, and apoptosis. This protein features a RING domain, which is characteristic of TRIM family members and is known to play a critical role in protein ubiquitination, thus regulating protein stability and function. The research surrounding TRIM14 has revealed its involvement in modulating inflammatory responses, particularly in the context of viral infections and autoimmune diseases. Additionally, studies have suggested that TRIM14 may influence various signaling pathways, including those related to NF-κB and interferon signaling, further underscoring its potential as a therapeutic target. However, the precise mechanisms through which TRIM14 exerts its effects remain unclear, prompting ongoing investigations into its role at the molecular level. Researchers are now focusing on generating recombinant TRIM14 proteins to facilitate these studies, which may provide insights into its structure-function relationships and interactions with other cellular components. By elucidating these aspects, scientists hope to uncover the therapeutic potential of TRIM14 in treating inflammatory conditions and other diseases linked to dysregulated immune responses, making it a promising area of study in molecular biology and immunology.
