Analytical Data
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基因名
TRIM68
- Application
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别名
TRIM68; GC109; RNF137; SS56; E3 ubiquitin-Protein ligase TRIM68; EC 2.3.2.27; RING finger Protein 137; RING-type E3 ubiquitin transferase TRIM68; SSA Protein SS-56; SS-56; Tripartite motif-containing Protein 68
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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
Q6AZZ1
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表达区间
1-485 aa
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氨基酸序列
MDPTALVEAI VEEVACPICM TFLREPMSID CGHSFCHSCL SGLWEIPGES QNWGYTCPLC RAPVQPRNLR PNWQLANVVE KVRLLRLHPG MGLKGDLCER HGEKLKMFCK EDVLIMCEAC SQSPEHEAHS VVPMEDVAWE YKWELHEALE HLKKEQEEAW KLEVGERKRT ATWKIQVETR KQSIVWEFEK YQRLLEKKQP PHRQLGAEVA AALASLQREA AETMQKLELN HSELIQQSQV LWRMIAELKE RSQRPVRWML QDIQEVLNRS KSWSLQQPEP ISLELKTDCR VLGLREILKT YAADVRLDPD TAYSRLIVSE DRKRVHYGDT NQKLPDNPER FYRYNIVLGS QCISSGRHYW EVEVGDRSEW GLGVCKQNVD RKEVVYLSPH YGFWVIRLRK GNEYRAGTDE YPILSLPVPP RRVGIFVDYE AHDISFYNVT DCGSHIFTFP RYPFPGRLLP YFSPCYSIGT NNTAPLAICS LDGED
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分子量
56.2 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
TRIM68, a member of the tripartite motif (TRIM) protein family, has garnered significant interest due to its potential roles in various cellular processes, including protein degradation, inflammation, and cell signaling. The TRIM family is characterized by its RING finger domain, which confers E3 ubiquitin ligase activity, thereby regulating protein turnover and homeostasis. Recent studies suggest that TRIM68 may play crucial roles in the immune response and cellular stress response, as well as in the pathology of certain diseases, including cancer and autoimmune disorders. By understanding the structural and functional characteristics of TRIM68, researchers aim to elucidate its molecular mechanisms and explore its potential as a therapeutic target. Recombining TRIM68 into a recombinant protein allows for detailed functional assays and structural studies that are critical for deciphering its interactions and pathways in vivo. The engineering of this protein thus serves as an essential step in advancing our knowledge of its biological significance and therapeutic applications. Overall, the study of TRIM68 is pivotal in uncovering new insights into cellular regulation and its implications in health and disease.
