Analytical Data
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Gene name
TR1
- Application
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Alternative Names
TR1；Translocating chain-associated membrane Protein 1-like 1
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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
Q8IYR6
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Expression Region
40-330aa
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AA Sequence
SNQPPGGGGGSGGDCPGGKGKSINCSELNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGDTYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRKHSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFVREASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQREDVYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFSILYVVPSRQKLTHV
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Molecular Weight
38.5 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
Related Products
Protein Description
TR1, or Thioredoxin-Related Protein 1, is a crucial protein involved in various biological processes, including redox regulation, signal transduction, and protein folding. It belongs to the thioredoxin family, which plays a vital role in maintaining the oxidative balance within cells. The enhanced understanding of TR1's structure and function has significant implications for cancer research, neurodegenerative diseases, and autoimmune disorders. Studies have shown that TR1 can interact with various cellular pathways, influencing cell proliferation, apoptosis, and stress responses. Moreover, its potential as a therapeutic target is being explored, particularly in the development of drugs aimed at modulating redox states in diseased tissues. Given the increasing evidence linking TR1 to disease pathology and its regulatory mechanisms, ongoing research focuses on elucidating its specific roles and mechanisms of action. By employing techniques such as gene editing, protein engineering, and high-throughput screening, researchers aim to uncover the multifaceted functions of TR1 and its contributions to health and disease. Understanding TR1 at both molecular and cellular levels may pave the way for innovative therapeutic strategies, ultimately enhancing treatment options for conditions where redox imbalances play a crucial role.
