Analytical Data
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Gene name
GLRX3
- Application
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Alternative Names
GLRX3；PICOT；TXNL2；Glutaredoxin-3
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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
O76003
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Expression Region
1-335aa
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AA Sequence
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
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Molecular Weight
64.3kDa
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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
GLRX3, or Glutaredoxin 3, is a member of the glutaredoxin family, known for its crucial role in redox regulation and cellular responses to oxidative stress. It serves as a thiol-disulfide oxidoreductase, facilitating the reduction of disulfide bonds and contributing to cellular redox homeostasis. Research into GLRX3 has gained momentum due to its implications in various diseases, including cancer and neurodegenerative disorders, where oxidative stress plays a significant role in pathogenesis. The protein's involvement in mitochondrial function and its potential role as a biomarker for oxidative stress-related diseases have further heightened interest in characterizing GLRX3. The recombinant expression of GLRX3 provides a valuable tool for studying its biochemical properties and functional mechanisms. By producing the protein in a controlled environment, researchers can investigate its interactions with other cellular components, elucidate its enzymatic activity, and explore its therapeutic potential. Moreover, understanding the structure-function relationship of GLRX3 can pave the way for the development of novel interventions targeting oxidative stress-related conditions. Overall, GLRX3 is emerging as a significant player in the field of redox biology, and ongoing studies aim to unlock its full potential in clinical applications.
