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Immunocytochemistry
ImmunohistochemistryAntibody data
- Antibody Data
- Antigen structure
- References [8]
- Comments [0]
- Validations
- Immunocytochemistry [1]
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- Product number
- HPA027104 - Provider product page
- Provider
- Atlas Antibodies
- Proper citation
- Atlas Antibodies Cat#HPA027104, RRID:AB_10601330
- Product name
- Anti-ADPRHL2
- Antibody type
- Polyclonal
- Description
- Polyclonal Antibody against Human ADPRHL2, Gene description: ADP-ribosylhydrolase like 2, Alternative Gene Names: ARH3, FLJ20446, Validated applications: IHC, ICC, Uniprot ID: Q9NX46, Storage: Store at +4°C for short term storage. Long time storage is recommended at -20°C.
- Reactivity
- Human
- Host
- Rabbit
- Conjugate
- Unconjugated
- Isotype
- IgG
- Vial size
- 100 µl
- Concentration
- 0.3 mg/ml
- Storage
- Store at +4°C for short term storage. Long time storage is recommended at -20°C.
- Handling
- The antibody solution should be gently mixed before use.
Submitted references Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesions
Serine-linked PARP1 auto-modification controls PARP inhibitor response
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair
Serine is the major residue for ADP-ribosylation upon DNA damage
Interplay of Histone Marks with Serine ADP-Ribosylation
Serine ADP-ribosylation reversal by the hydrolase ARH3
Zentout S, Imburchia V, Chapuis C, Duma L, Schützenhofer K, Prokhorova E, Ahel I, Smith R, Huet S
Proceedings of the National Academy of Sciences 2024;121(25)
Proceedings of the National Academy of Sciences 2024;121(25)
Nie L, Wang C, Huang M, Liu X, Feng X, Tang M, Li S, Hang Q, Teng H, Shen X, Ma L, Gan B, Chen J
2024
2024
Serine-linked PARP1 auto-modification controls PARP inhibitor response
Prokhorova E, Zobel F, Smith R, Zentout S, Gibbs-Seymour I, Schützenhofer K, Peters A, Groslambert J, Zorzini V, Agnew T, Brognard J, Nielsen M, Ahel D, Huet S, Suskiewicz M, Ahel I
Nature Communications 2021;12(1)
Nature Communications 2021;12(1)
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Hendriks I, Buch-Larsen S, Prokhorova E, Elsborg J, Rebak A, Zhu K, Ahel D, Lukas C, Ahel I, Nielsen M
Nature Communications 2021;12(1)
Nature Communications 2021;12(1)
Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair
Hanzlikova H, Prokhorova E, Krejcikova K, Cihlarova Z, Kalasova I, Kubovciak J, Sachova J, Hailstone R, Brazina J, Ghosh S, Cirak S, Gleeson J, Ahel I, Caldecott K
Nature Communications 2020;11(1)
Nature Communications 2020;11(1)
Serine is the major residue for ADP-ribosylation upon DNA damage
Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I
eLife 2018;7
eLife 2018;7
Interplay of Histone Marks with Serine ADP-Ribosylation
Bartlett E, Bonfiglio J, Prokhorova E, Colby T, Zobel F, Ahel I, Matic I
Cell Reports 2018;24(13):3488-3502.e5
Cell Reports 2018;24(13):3488-3502.e5
Serine ADP-ribosylation reversal by the hydrolase ARH3
Fontana P, Bonfiglio J, Palazzo L, Bartlett E, Matic I, Ahel I
eLife 2017;6
eLife 2017;6
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Supportive validation
- Submitted by
- Atlas Antibodies (provider)
- Main image
- Experimental details
- Immunofluorescent staining of human cell line A-431 shows localization to nucleoplasm.
- Sample type
- Human
