Analytical Data
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基因名
TRIM38
- Application
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别名
TRIM38; RNF15; RORET; E3 ubiquitin-Protein ligase TRIM38; EC 2.3.2.27; RING finger Protein 15; RING-type E3 ubiquitin transferase TRIM38; Tripartite motif-containing Protein 38; Zinc finger Protein RoRet
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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
O00635
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表达区间
1-465 aa
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氨基酸序列
MASTTSTKKM MEEATCSICL SLMTNPVSIN CGHSYCHLCI TDFFKNPSQK QLRQETFCCP QCRAPFHMDS LRPNKQLGSL IEALKETDQE MSCEEHGEQF HLFCEDEGQL ICWRCERAPQ HKGHTTALVE DVCQGYKEKL QKAVTKLKQL EDRCTEQKLS TAMRITKWKE KVQIQRQKIR SDFKNLQCFL HEEEKSYLWR LEKEEQQTLS RLRDYEAGLG LKSNELKSHI LELEEKCQGS AQKLLQNVND TLSRSWAVKL ETSEAVSLEL HTMCNVSKLY FDVKKMLRSH QVSVTLDPDT AHHELILSED RRQVTRGYTQ ENQDTSSRRF TAFPCVLGCE GFTSGRRYFE VDVGEGTGWD LGVCMENVQR GTGMKQEPQS GFWTLRLCKK KGYVALTSPP TSLHLHEQPL LVGIFLDYEA GVVSFYNGNT GCHIFTFPKA SFSDTLRPYF QVYQYSPLFL PPPGD
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分子量
53.4 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
TRIM38, a member of the tripartite motif (TRIM) family of proteins, has gained attention in recent years due to its critical role in regulating various cellular processes, including immune response, inflammation, and tumorigenesis. This protein possesses a RING finger domain, which is characteristic of E3 ubiquitin ligases, allowing it to modulate protein stability and activity through ubiquitination. Studies have indicated that TRIM38 can target various signaling pathways, notably the NF-κB pathway, thereby influencing the expression of pro-inflammatory cytokines. Its dysregulation has been implicated in several diseases, including cancer, where it may contribute to tumor progression and immune evasion. Additionally, TRIM38 has been shown to interact with various viral proteins, highlighting its potential role in innate immune responses against viral infections. Given the importance of TRIM38 in both normal physiological functions and pathological conditions, researchers have focused on developing recombinant TRIM38 proteins to study their mechanisms of action, interactions with other cellular components, and therapeutic potentials. Understanding the structure and function of TRIM38 through recombinant technology could pave the way for novel therapeutic strategies targeting TRIM38-related pathways in diseases such as cancer and viral infections. This research has important implications for developing targeted therapies and enhancing our understanding of the molecular mechanisms underlying immune regulation and oncogenesis.
