Analytical Data
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Gene name
GLRX5
- Application
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Alternative Names
GLRX5；C14orf87;Glutaredoxin-related Protein 5. mitochondrial
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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
Q86SX6
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Expression Region
32-157aa
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AA Sequence
AGSGAGGGG SAEQLDALVK KDKVVVFLKG TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK
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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
GLRX5, or Glutaredoxin 5, is a crucial protein implicated in iron-sulfur cluster biogenesis and cellular redox homeostasis. Its significance has been underscored in various biological processes, particularly in mitochondrial function, where it plays a pivotal role in the assembly of iron-sulfur clusters essential for the activity of numerous mitochondrial proteins. The disturbance of GLRX5 function is linked to a variety of pathological conditions, including neurodegenerative diseases and metabolic disorders, making it a potential target for therapeutic interventions. Recent studies have highlighted the necessity for understanding the molecular mechanisms underlying GLRX5's role in cellular metabolism and oxidative stress, driving the need for the expression and characterization of recombinant GLRX5 proteins. By producing this protein in a controlled laboratory setting, researchers aim to elucidate its structural properties, interaction partners, and enzymatic functions. This knowledge not only enhances our understanding of the protein's biological roles but also contributes to the development of novel strategies for mitigating diseases associated with GLRX5 dysfunction. The study of recombinant GLRX5 is thus positioned at the intersection of basic biochemistry and clinical relevance, promising to yield insights into both fundamental cellular processes and potential therapeutic avenues.
