Analytical Data
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Gene name
RNF8
- Application
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Alternative Names
RNF8;KIAA0646;E3 ubiquitin-Protein ligase RNF8
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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
O76064
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Expression Region
1-485aa
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AA Sequence
MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQL VSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSI HQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKEL RTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPS DNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFK VTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLC AEQAQQQARVEQLEKTFQEEEQHLQGLEIAQGEKDLKQQLAQALQEHWAL MEELNRSKKDFEAIIQAKNKELEQTKEEKEKMQAQKEEVLSHMNDVLENE LQCIICSEYFIEAVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKTYS LVLDNCINKMVNNLSSEVKERRIVLIRERKAKRLF
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Molecular Weight
79 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
RNF8 (Ring Finger Protein 8) is an E3 ubiquitin ligase that plays a crucial role in the DNA damage response and repair mechanisms. It is involved in the recognition and signaling of DNA double-strand breaks (DSBs), a critical form of genomic instability linked to various cancers. RNF8 is essential for the recruitment of DNA repair proteins, such as BRCA1 and 53BP1, to sites of damage, thereby facilitating the repair process. Dysregulation of RNF8 has been associated with impaired DNA repair capacity, leading to increased susceptibility to tumorigenesis. Given its pivotal role in maintaining genomic integrity, RNF8 has gained attention as a potential therapeutic target in cancer treatment. Research into recombinant RNF8 protein aims to understand its structure-function relationships, regulatory mechanisms, and interactions with other repair proteins. This knowledge could pave the way for developing novel strategies to enhance DNA repair pathways in cancer cells, potentially improving the efficacy of existing therapies and advancing personalized medicine approaches. Furthermore, investigating RNF8’s function may reveal insights into the molecular basis of hereditary cancer syndromes linked to defective DNA repair mechanisms. Overall, the study of recombinant RNF8 protein represents a significant avenue for unlocking new insights into the cellular response to DNA damage and the development of cancer therapies.











