Analytical Data
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Gene name
TRXB
- Application
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Alternative Names
TRXB；GRIM12；Thioredoxin reductase 1. cytoplasmic
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Species
E.coli
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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
P0A9P4
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Expression Region
2-321aa
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AA Sequence
GTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K
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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
TRXB, or thioredoxin B, is a protein involved in redox regulation and cellular stress response, primarily found in various organisms, including bacteria and eukaryotes. Research into TRXB has gained momentum due to its critical role in maintaining protein structure and function through the modulation of disulfide bond formation. This is particularly significant in the context of cancer and other diseases where oxidative stress plays a pivotal role in disease progression. The ability of TRXB to regulate redox homeostasis makes it a target for therapeutic interventions aimed at modulating oxidative stress-related pathways. Furthermore, studies have shown that TRXB can influence cell signaling, proliferation, and apoptosis, which further underscores its importance in cellular health and disease. Advances in recombinant protein technology have enabled the production of TRXB in sufficient quantities for detailed biochemical studies, facilitating the exploration of its functional mechanisms and interactions within the cell. By engineering TRXB as a recombinant protein, researchers aim to investigate its potential as a biomarker for disease states and a target for novel drug development. Overall, TRXB represents a crucial focus in cell biology and therapeutic research, with the potential to inform innovative approaches to combating oxidative stress-related diseases.
