Analytical Data
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基因名
torA
- Application
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别名
torA；DQ2；DYT1；TA；Torsin-1A
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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
P33225
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表达区间
99-572aa
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氨基酸序列
RIRYPMVRVDWLRKRHLSDTSQRGDNRFVRVSWDEALDMFYEELERVQKTHGPSALLTASGWQSTGMFHNASGMLAKAIALHGNSVGTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDLLKNQQANWWCPDHDVYEYYAQLKAKVAAGEIEVISIDPVVTSTHEYLGREHVKHIAVNPQTDVPLQLALAHTLYSENLYDKNFLANYCVGFEQFLPYLLGEKDGQPKDAAWAEKLTGIDAETIRGLARQMAANRTQIIAGWCVQRMQHGEQWAWMIVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGVILSGFSGSTSIPPVHDNSDYKGYSSTIPIARFIDAILEPGKVINWNGKSVKLPPLKMCIFAGTNPFHRHQQINRIIEGLRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQYGNHSNRGIIAMKQVVPPQFEARNDFDIFRELCR
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分子量
60.6 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
The study of TorA, a protein associated with the bacterial signal transduction process, has garnered significant attention due to its potential implications in understanding microbial physiology and pathogenicity. TorA, a membrane-associated protein involved in the respiratory pathway of specific bacteria, facilitates the reduction of trimethylamine N-oxide (TMAO) and plays a critical role in anaerobic respiration. Research on TorA has expanded in recent years, as it serves not only as a key player in energy metabolism but also as a potential target for antimicrobial strategies. Investigating the structure, function, and regulation of TorA can provide insights into the adaptive mechanisms that enable bacteria to thrive in diverse environments, including those that are hostile. Moreover, by elucidating the molecular pathways that TorA influences, scientists hope to better understand its role in bacterial survival and its contributions to disease processes. This exploration is particularly vital as antibiotic resistance continues to pose a significant challenge in clinical settings. Consequently, the characterization of TorA offers valuable information that could aid in the development of novel therapeutic approaches, enhancing our capacity to combat bacterial infections. Overall, the ongoing research on TorA exemplifies the intersection of microbiology, biochemistry, and pharmacology, highlighting the necessity for continuous exploration of bacterial proteins in the quest for effective treatments against resistant pathogens.
