Analytical Data
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Gene name
BRCC36
- Application
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Alternative Names
C6.1A; BRCC36; C6.1A; CXorf53; Lys-63-specific deubiquitinase BRCC36; BRCA1-A complex subunit BRCC36; BRISC complex subunit BRCC36
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P46736
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Expression Region
Gln7~Gly148
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Molecular Weight
20kDa
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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
BRCC36, a member of the BRCA1-A complex, plays a pivotal role in the DNA damage response and repair mechanisms, particularly in the context of homologous recombination. Alterations in BRCC36 have been associated with various cancers, underscoring its importance in maintaining genomic stability. Researchers have focused on the structural and functional characterization of BRCC36 to better understand its interactions within the cellular environment. Notably, BRCC36 exhibits deubiquitinating activity which is crucial for the regulation of protein stability during the DNA repair processes. Investigations into its reconstitution as a recombinant protein have aimed to elucidate its biochemical properties and functional relationships with other proteins involved in the DNA damage response. By employing techniques such as X-ray crystallography and mass spectrometry, scientists seek to map the interaction networks and delineate the mechanistic pathways facilitated by BRCC36. This research not only enhances our understanding of BRCC36's fundamental biological roles but also opens avenues for potential therapeutic interventions targeting its dysregulation in cancer.
