Antibody data
- Antibody Data
- Antigen structure
- References [6]
- Comments [0]
- Validations [0]
Submit
Validation data
Reference
Comment
Report error
- Product number
- 14-6667-80 - Provider product page
- Provider
- Invitrogen Antibodies
- Product name
- Anti-PARP1 (cleaved Asp214) Monoclonal Antibody (HC2R8), eBioscience™
- Antibody type
- Monoclonal
- Antigen
- Other
- Description
- Description: This HC2R8 monoclonal antibody reacts with human poly (ADP-ribose) polymerase (PARP1). This ubiquitous 116 kDa nuclear enzyme is involved in DNA repair. During apoptosis, active caspases -3, -6 and -7 cleave PARP1 after Asp214, thereby inactivating PARP1 and generating two apoptotic fragments sized 85 kDa and 25 kDa. The HC2R8 antibody specifically recognizes both the cleaved and non-cleaved forms of PARP. Applications Reported: This HC2R8 antibody has been reported for use in immunoblotting (WB). Applications Tested: This HC2R8 antibody has been tested by immunoblotting of staurosporine-treated Jurkat cells. This can be used at less than or equal to 0.1 µg/mL. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest. Purity: Greater than 90%, as determined by SDS-PAGE. Aggregation: Less than 10%, as determined by HPLC. Filtration: 0.2 µm post-manufacturing filtered.
- Reactivity
- Human
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- HC2R8
- Vial size
- 25 µg
- Concentration
- 0.5 mg/mL
- Storage
- 4° C
Submitted references Identification of an acetylation-dependant Ku70/FLIP complex that regulates FLIP expression and HDAC inhibitor-induced apoptosis.
The role of proteases during apoptosis.
Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase.
Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study.
Production and characterization of monoclonal antibodies specific for the functional domains of poly(ADP-ribose) polymerase.
Poly(ADP-ribose) polymerase is a zinc metalloenzyme.
Kerr E, Holohan C, McLaughlin KM, Majkut J, Dolan S, Redmond K, Riley J, McLaughlin K, Stasik I, Crudden M, Van Schaeybroeck S, Fenning C, O'Connor R, Kiely P, Sgobba M, Haigh D, Johnston PG, Longley DB
Cell death and differentiation 2012 Aug;19(8):1317-27
Cell death and differentiation 2012 Aug;19(8):1317-27
The role of proteases during apoptosis.
Patel T, Gores GJ, Kaufmann SH
FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1996 Apr;10(5):587-97
FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1996 Apr;10(5):587-97
Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase.
Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM
Cell 1995 Jun 2;81(5):801-9
Cell 1995 Jun 2;81(5):801-9
Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study.
Lamarre D, Talbot B, de Murcia G, Laplante C, Leduc Y, Mazen A, Poirier GG
Biochimica et biophysica acta 1988 Jul 13;950(2):147-60
Biochimica et biophysica acta 1988 Jul 13;950(2):147-60
Production and characterization of monoclonal antibodies specific for the functional domains of poly(ADP-ribose) polymerase.
Lamarre D, Talbot B, Leduc Y, Muller S, Poirier G
Biochemistry and cell biology = Biochimie et biologie cellulaire 1986 Apr;64(4):368-76
Biochemistry and cell biology = Biochimie et biologie cellulaire 1986 Apr;64(4):368-76
Poly(ADP-ribose) polymerase is a zinc metalloenzyme.
Zahradka P, Ebisuzaki K
European journal of biochemistry 1984 Aug 1;142(3):503-9
European journal of biochemistry 1984 Aug 1;142(3):503-9
No comments: Submit comment
No validations: Submit validation data