Product: Procainamide (hydrochloride)
RNF8 Antibody Summary
| Immunogen |
Antibody was raised against a 14 amino acid synthetic peptide near the carboxy terminus of human RNF8. The immunogen is located within amino acids 330 – 380 of RNF8.
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| Specificity |
At least three isoforms of RNF8 are known to exist; this antibody will detect all three isoforms.
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| Clonality |
Polyclonal
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| Host |
Rabbit
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| Gene |
RNF8
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| Purity |
Immunogen affinity purified
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Applications/Dilutions
| Dilutions |
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| Theoretical MW |
50 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| Control Peptide |
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Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
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| Buffer |
PBS
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| Preservative |
0.02% Sodium Azide
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| Concentration |
1 mg/ml
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| Purity |
Immunogen affinity purified
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Alternate Names for RNF8 Antibody
- ActA Binding Protein 2
- C3HC4-type zinc finger protein
- EC 6.3.2
- EC 6.3.2.-
- FLJ12013
- KIAA0646UBC13/UEV-interacting ring finger protein
- ring finger protein (C3HC4 type) 8
- ring finger protein 8E3 ubiquitin-protein ligase RNF8
- RNF8
Background
RNF8 was identified as a ubiquitin ligase (E3) containing a RING finger motif and a FHA domain. This protein has been shown to interact with several class II ubiquitin-conjugating enzymes including UBE2E1/UBCH6, UBE2E2, and UBE2E3. RNF8 assembles at DNA double-strand breaks (DSBs) via interactions though the FHA domain with the adaptor protein MDC1, resulting in an increase in DSB-associated H2A histone ubiquitinations mediated by the associated ubiquitin ligase RNF168 followed by the accumulation of 53BP1 and BRCA1 repair proteins. Together with RNF168, RNF8 plays an integral part of class switch recombination in B cells, allowing the production of several classes of antibodies, through the recruitment of 53BP1 and BRCA1 to the DSB sites.