Analytical Data
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Gene name
grxB
- Application
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Alternative Names
grxB; b1064; JW1051Glutaredoxin 2; Grx2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AC59
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Expression Region
1-215aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMKLYIYDHCPYCLKARMIFGLKNIPVELHVLLNDDAETPTRMVGQKQVPILQKDDSRYMPESMDIVHYVDKLDGKPLLTGKRSPAIEEWLRKVNGYANKLLLPRFAKSAFDEFSTPAARKYFVDKKEASAGNFADLLAHSDGLIKNISDDLRALDKLIVKPNAVNGELSEDDIQLFPLLRNLTLVAGINWPSRVADYRDNMAKQTQINLLSSMAI
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Molecular Weight
26.5 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
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Protein Description
The study of recombinant GRXB (glutaredoxin B) proteins is rooted in the broader field of redox biology and protein engineering. Glutaredoxins are small, oxidoreductase enzymes that play crucial roles in maintaining cellular redox homeostasis by catalyzing the reduction of disulfides and the modulation of protein thiol states. GRXB, in particular, has garnered attention due to its potential involvement in regulating oxidative stress responses, protein folding, and various signaling pathways. The recombinant expression of GRXB allows researchers to produce this protein in a controlled environment, facilitating studies on its structural and functional properties. Understanding GRXB's biochemical mechanisms can provide insights into its role in disease processes, such as cancer and neurodegeneration, where redox imbalance contributes to pathophysiology. Additionally, recombinant GRXB can be utilized in biotechnological applications, including drug development and enzyme engineering, owing to its ability to interact with various substrates. This research aims to elucidate the mechanistic details of GRXB's activity and its interactions with cellular components, paving the way for potential therapeutic strategies targeting redox regulation.
