Analytical Data
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Gene name
COPS5
- Application
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Alternative Names
38 kDa Mov34 homolog; COP9 (constitutive photomorphogenic) homolog subunit 5; COP9 constitutive photomorphogenic homolog subunit 5; COP9 signalosome complex subunit 5; COP9 signalosome subunit 5; Cop9 subunit 5; COPS 5
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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
Q92905
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Expression Region
1-344aa
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AA Sequence
MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS
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Molecular Weight
62.48 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
Related Products
Protein Description
COQ2, or Coenzyme Q10 (CoQ10) biosynthesis protein 2, plays a crucial role in the synthesis of ubiquinone, an essential component of the electron transport chain in mitochondria, which is vital for ATP production. Impaired COQ2 function has been linked to various mitochondrial disorders, including primary coenzyme Q10 deficiency, leading to severe clinical symptoms such as neurological deficits and muscle weakness. The study of COQ2 recombinant protein is pivotal for understanding its enzymatic mechanisms and the regulation of CoQ10 biosynthesis. Research into COQ2 not only provides insights into the molecular basis of related pathologies but also offers potential therapeutic avenues for managing conditions associated with CoQ10 deficiency. By producing and characterizing COQ2 recombinant protein, scientists can investigate its interactions with other biosynthetic enzymes, identify the effects of mutations on its activity, and develop small molecule modulators that could enhance CoQ10 levels in affected individuals. Furthermore, such studies contribute to the broader understanding of mitochondrial dysfunction and its implications for various diseases, including neurodegenerative disorders, cardiomyopathies, and aging-related conditions. Overall, the exploration of COQ2 recombinant protein is a promising area of research that bridges basic science and potential clinical applications, aiming to improve therapeutic strategies for patients suffering from CoQ10-related diseases.
