Analytical Data
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基因名
TR
- Application
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别名
TR；CIP4；STOT；STP；Cdc42-interacting Protein 4
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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
Q8IYR6
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表达区间
40-330aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSSNQPPGGGGGSGGDCPGGKGKSINCSE LNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGD TYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRK HSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFV REASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQRED VYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFS ILYVVPSRQKLTHV
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分子量
34 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
TR (Tetratricopeptide Repeat) proteins are an important class of proteins characterized by the presence of tandem repeats of approximately 34 amino acids that form a helix-loop-helix structure. These proteins play crucial roles in various biological processes, including protein-protein interactions, molecular chaperoning, and signal transduction. The study of TR proteins has gained significant attention due to their involvement in critical cellular functions and their implications in various diseases. For instance, dysregulation of TR proteins has been linked to cancer, neurodegenerative disorders, and other pathologies, making them potential targets for therapeutic intervention. Research into TR protein structure and function utilizes a range of techniques, including crystallography, NMR spectroscopy, and advanced imaging methods, to elucidate their mechanisms of action. Additionally, the versatility of TR repeats as modular interaction motifs has opened avenues for engineering novel proteins with specific functionalities, enhancing their potential applications in biotechnology and medicine. As our understanding of TR proteins deepens, it continues to provide insights into fundamental biological processes and offers promising strategies for disease treatment and prevention.
