Analytical Data
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Gene name
BRCC3
- Application
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Alternative Names
BR;CA1-A complex subunit BR;CC36BR;CA1/BR;CA2-containing complex subunit 3BR;CA1/BR;CA2-containing complex subunit 36BRISC complex subunit BR;CC36
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Species
Human
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Source
E. coli
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Tag
N- His-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P46736
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Expression Region
2-316aa
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Molecular Weight
65.9 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
BRCC3 (Brat Like Protein 3) is a crucial deubiquitinating enzyme that plays a significant role in the regulation of protein homeostasis, DNA repair, and cell signaling pathways. Research has shown that BRCC3 is involved in various cellular processes, including the mitigation of oxidative stress and the maintenance of genome stability, which are vital for cellular survival and function. The protein has been implicated in cancer biology, particularly in enhancing the survival of cancer cells under stress and in resistance to chemotherapeutic agents. Given its importance, understanding the structural and functional aspects of BRCC3 is essential for elucidating its role in tumorigenesis and potential therapeutic interventions. Recent studies have focused on the recombinant expression and purification of BRCC3 to characterize its enzymatic activity and interactions with other cellular proteins. Through the use of advanced techniques such as X-ray crystallography and mass spectrometry, researchers aim to uncover the molecular mechanisms by which BRCC3 exerts its effects in the cell, offering insights into new drug development strategies targeting BRCC3 for cancer therapy and potentially other diseases linked to its dysregulation. Furthermore, the study of BRCC3 is instrumental in advancing our knowledge of the broader family of deubiquitinating enzymes and their implications in human health and disease.
