Anti-Human PARP1 (Cleaved) PE

Also known as: poly ADP-ribose polymerase

Clone: HLNC4

RUO: For Research Use Only. Not for use in diagnostic procedures.

SKU# 12-6668

Cat. No. Size
12-6668-41 25 tests
12-6668-42 100 tests
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Data for Anti-Human PARP1 (Cleaved) PE.

Jurkat cells were left unstimulated (left) or stimulated for 20 hours with Anti-Human CD95...View More

  • Data for Anti-Human PARP1 (Cleaved) PE.
Description

Description: This HLNC4 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 HLNC4 antibody specifically recognizes the 85 kDa PARP1 fragment produced after cleavage and does not recognize the full-length 116 kDa protein.The following peptide was used as the immunogen: NH2-GVDEVAKKKSKKEKDC-COOH.

Details
Host Mouse
Isotype IgG2b, kappa
Reactivity Human
Conjugate PE
Laser Blue Laser, Green Laser, Yellow-Green Laser
Emit 575 nm
Excite 488 - 561 nm
Reported Applications Intracellular Staining Followed by Flow Cytometric Analysis
Documentation

For complete product information, please download the TDS or IFU document.

TDS Link Download TDS
Additional Formats
Cat. No. Name Excite Emit Application Reg.
53-6668 Anti-Human PARP1 (Cleaved) Alexa Fluor® 488 488 nm 519 nm FC RUO
14-6668 Anti-Human PARP1 (Cleaved) Purified WB RUO
References

References: Patel T, Gores GJ, Kaufmann SH. The role of proteases during apoptosis. FASEB J. 1996. Apr;10(5):587-97. Review.

Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995. Jun 2;81(5):801-9.

Lamarre D, Talbot B, de Murcia G, Laplante C, Leduc Y, Mazen A, Poirier GG. Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study. Biochim Biophys Acta. 1988. Jul 13;950(2):147-60.

Lamarre D, Talbot B, Leduc Y, Muller S, Poirier G. Production and characterization of monoclonal antibodies specific for the functional domains of poly(ADP-ribose) polymerase. Biochem Cell Biol. 1986. Apr;64(4):368-76.

Zahradka P, Ebisuzaki K. Poly(ADP-ribose) polymerase is a zinc metalloenzyme. Eur. J. Biochem. 1984.142: 503-509.


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