Analytical Data
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Gene name
RNF8
- Application
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Alternative Names
RING finger protein 8 (RING-type E3 ubiquitin transferase RNF8)
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Species
Human
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O76064
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Expression Region
1-485aa
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Molecular Weight
59.4 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
RNF8 is a crucial E3 ubiquitin ligase involved in DNA damage repair and the regulation of cellular responses to genotoxic stress. It plays a significant role in the ubiquitination processes following DNA double-strand breaks, facilitating the repair mechanisms through the recruitment of other repair factors to the site of damage. Mutations or dysregulation of RNF8 have been linked to various cancers and genetic disorders, highlighting its importance in maintaining genomic stability. Furthermore, RNF8 is known to interact with several key proteins in the DNA damage response pathway, underscoring its role as a pivotal regulator of cellular repair processes. Recent studies have focused on characterizing the structural and functional properties of RNF8, aiming to elucidate its mechanism of action and how it modulates protein interactions. Understanding RNF8's function at the molecular level may provide insights into targeted therapeutic strategies for diseases characterized by defective DNA repair. Additionally, research into RNF8 can enhance our comprehension of the broader network of ubiquitin signaling in cellular processes, potentially revealing novel intervention points in cancer treatment and the management of other conditions associated with DNA repair deficiencies.
