Analytical Data
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基因名
TRAIP
- Application
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别名
TRAIP;RNF206;TRIP;E3 ubiquitin-Protein ligase TRAIP
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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
Q9BWF2
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表达区间
1-469aa
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氨基酸序列
MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS
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分子量
58.8 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
TRAIP (TRAF-interacting protein) is an important protein involved in various cellular processes, including DNA damage response, cell cycle regulation, and apoptosis. Research on TRAIP protein has gained significant attention due to its role in maintaining genomic stability and its potential implications in cancer biology. TRAIP is known to function as an E3 ubiquitin ligase, which facilitates the attachment of ubiquitin molecules to target proteins, thereby regulating their degradation or activity. Dysregulation of TRAIP has been associated with several cancers, including breast and colorectal cancers, highlighting its potential as a biomarker or therapeutic target. The study of TRAIP's structure and function at the molecular level is crucial for understanding its role in tumorigenesis and therapeutic resistance. Recent advancements in protein engineering and structural biology have enabled researchers to characterize TRAIP more comprehensively, paving the way for innovative strategies to modulate its activity. By elucidating the mechanisms underlying TRAIP's function, scientists aim to develop targeted therapies that may enhance treatment efficacy and overcome resistance in cancer patients. Understanding TRAIP’s role in cellular signaling pathways and its interactions with other proteins could provide insights into novel cancer treatment approaches and the design of small molecule inhibitors that could selectively modulate its function. Hence, ongoing research into TRAIP offers promising avenues for cancer therapy and emphasizes the need for a deeper exploration of its biological significance and therapeutic potential.












