Analytical Data
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Gene name
torA
- Application
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Alternative Names
torA；DQ2；DYT1；TA；Torsin-1A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33225
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Expression Region
99-572aa
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AA Sequence
RIRYPMVRVDWLRKRHLSDTSQRGDNRFVRVSWDEALDMFYEELERVQKTHGPSALLTASGWQSTGMFHNASGMLAKAIALHGNSVGTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDLLKNQQANWWCPDHDVYEYYAQLKAKVAAGEIEVISIDPVVTSTHEYLGREHVKHIAVNPQTDVPLQLALAHTLYSENLYDKNFLANYCVGFEQFLPYLLGEKDGQPKDAAWAEKLTGIDAETIRGLARQMAANRTQIIAGWCVQRMQHGEQWAWMIVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGVILSGFSGSTSIPPVHDNSDYKGYSSTIPIARFIDAILEPGKVINWNGKSVKLPPLKMCIFAGTNPFHRHQQINRIIEGLRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQYGNHSNRGIIAMKQVVPPQFEARNDFDIFRELCR
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Molecular Weight
60.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
