Analytical Data
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Gene name
Trx2
- Application
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Alternative Names
Trx2；HRX2；KIAA0304；MLL2；Histone-lysine N-methyltransferase 2B
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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
P10202
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Expression Region
1-318aa
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AA Sequence
MLADGFETDIAIPSGISRPDAAALQRCEGRVVFLPTIRRQLTLADVAHESFVSGGVSPDTLGLLLAYRRRFPAVITRVLPTRIVACPLDVGLTHAGTVNLRNTSPVDLCNGDPISLVPPVFEGQATDVRLDSLDLTLRFPVPLPSPLAREIVARLVARGIRDLNPSPRNPGGLPDLNVLYYNGSRLSLLADVQQLGPVNAELRSLVLNMVYSITEGTTIILTLIPRLFALSAQDGYVNALLQMQSVTREAAQLIHPEAPALMQDGERRLPLYEALVAWLTHAGQLGDTLALAPVVRVCTFDGAAVVRSGDMAPVIRYP
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Molecular Weight
41.2 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
TRX2, or Thioredoxin 2, is a mitochondrial protein that plays a crucial role in cellular redox homeostasis and the regulation of oxidative stress. As an important antioxidant, TRX2 is involved in maintaining mitochondrial function and protecting cells from oxidative damage, which is implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. The study of TRX2 recombinant protein has gained significant interest due to its potential therapeutic applications. By understanding its structure and function at a molecular level, researchers aim to elucidate the mechanisms behind its antioxidant properties and its interactions with other cellular components. Recombinant techniques allow for the production of TRX2 in sufficient quantities for detailed biochemical studies. These investigations can reveal how TRX2 modulates signaling pathways related to redox balance and its role in apoptosis and cell survival. Moreover, exploring the post-translational modifications of TRX2 and identifying its specific partners can provide insights into mitochondrial dynamics and the cellular response to stress. Overall, the research on TRX2 recombinant protein not only enhances our understanding of mitochondrial biology but also opens avenues for the development of novel therapeutic strategies targeting oxidative stress-related pathologies.
