Analytical Data
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基因名
TRIM31
- Application
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别名
TRIM31; C6orf13; RNF; E3 ubiquitin-Protein ligase TRIM31; EC 2.3.2.27; RING-type E3 ubiquitin transferase TRIM31; Tripartite motif-containing Protein 31
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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
Q9BZY9
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表达区间
1-425 aa
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氨基酸序列
MASGQFVNKL QEEVICPICL DILQKPVTID CGHNFCLKCI TQIGETSCGF FKCPLCKTSV RKNAIRFNSL LRNLVEKIQA LQASEVQSKR KEATCPRHQE MFHYFCEDDG KFLCFVCRES KDHKSHNVSL IEEAAQNYQG QIQEQIQVLQ QKEKETVQVK AQGVHRVDVF TDQVEHEKQR ILTEFELLHQ VLEEEKNFLL SRIYWLGHEG TEAGKHYVAS TEPQLNDLKK LVDSLKTKQN MPPRQLLEDI KVVLCRSEEF QFLNPTPVPL ELEKKLSEAK SRHDSITGSL KKFKDQLQAD RKKDENRFFK SMNKNDMKSW GLLQKNNHKM NKTSEPGSSS AGGRTTSGPP NHHSSAPSHS LFRASSAGKV TFPVCLLASY DEISGQGASS QDTKTFDVAL SEELHAALSE WLTAIRAWFC EVPSS
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分子量
48.2 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
TRIM31, a member of the TRIM (tripartite motif-containing) protein family, has garnered significant attention in recent years due to its diverse roles in cellular processes and disease mechanisms. TRIM proteins are characterized by their tripartite structure, which typically includes a RING domain, one or two B-box motifs, and a coiled-coil domain, allowing them to function in ubiquitination, signal transduction, and transcriptional regulation. TRIM31, in particular, has been implicated in the regulation of immune responses, inflammation, and tumorigenesis. Studies suggest that TRIM31 can modulate the activity of various signaling pathways, including the NF-kB and MAPK pathways, which are crucial for immune and inflammatory responses. Additionally, aberrant expression of TRIM31 has been linked to several cancers, making it a potential biomarker and therapeutic target. Research on TRIM31 has focused on elucidating its molecular mechanisms and interactions within the cell, particularly in the context of autoimmune diseases and cancer. Understanding the functional roles and regulatory networks of TRIM31 will not only enhance our knowledge of its biological significance but may also open new avenues for developing targeted therapies against diseases associated with its dysregulation. Overall, the study of TRIM31 represents a promising frontier in the exploration of protein functional dynamics and their implications in human health and disease.
