PARP1 Antibody (F-2): sc-8007

PARP-1 Antibody (F-2) is a mouse monoclonal IgG2a kappa light chain antibody designed to target the C-terminal region of human PARP-1 by recognizing amino acids 764-1014. PARP-1 monoclonal antibody (F-2) effectively detects both the full-length PARP-1 protein and its C-terminal cleavage product, making PARP-1 (F-2) antibody a valuable tool for various applications including western blotting, immunoprecipitation, immunofluorescence, immunohistochemistry on paraffin-embedded tissues, and ELISA. PARP-1 (Poly (ADP-ribose) polymerase 1), also called ARTD1, Adprt, and Parp1, is a crucial nuclear enzyme that plays a central role in the detection and repair of DNA single-strand breaks through the base excision repair pathway. Upon sensing DNA damage, PARP-1 binds to the damaged DNA and catalyzes the transfer of ADP-ribose units from NAD⁺ to itself and other target proteins in a process known as PARylation. This modification facilitates chromatin remodeling and the recruitment of additional DNA repair machinery, thereby maintaining genomic integrity and preventing mutations that could lead to diseases such as cancer. The structural organization of PARP-1 includes a DNA-binding domain that recognizes DNA damage, an automodification domain that allows for self-regulation through PARylation, and a catalytic domain responsible for enzymatic activity, ensuring a prompt and efficient response to DNA damage. Additionally, PARP-1 undergoes post-translational modifications, including automodification and cleavage by caspases during apoptosis. PARP-1 interacts with several key proteins involved in DNA repair and chromatin structure, such as XRCC1, DNA ligase III, DNA polymerase β, and histones, highlighting an essential role in coordinating the DNA damage response and preserving genomic stability. By utilizing PARP-1 mouse monoclonal antibody (F-2), researchers can study the intricate mechanisms of DNA repair, apoptosis, and the maintenance of genomic integrity, making anti-PARP-1 antibody (F-2) useful for advancements in molecular biology and medical research.

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PARP1 Antibody (F-2) References:

1. Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability.  |  d'Adda di Fagagna, F., et al. 1999. Nat Genet. 23: 76-80. PMID: 10471503
2. A cellular defense pathway regulating transcription through poly(ADP-ribosyl)ation in response to DNA damage.  |  Vispe, S., et al. 2000. Proc Natl Acad Sci U S A. 97: 9886-91. PMID: 10944198
3. DNA excision repair and DNA damage-induced apoptosis are linked to Poly(ADP-ribosyl)ation but have different requirements for p53.  |  Beneke, R., et al. 2000. Mol Cell Biol. 20: 6695-703. PMID: 10958667
4. The world according to PARP.  |  Smith, S. 2001. Trends Biochem Sci. 26: 174-9. PMID: 11246023
5. Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death.  |  Herceg, Z. and Wang, ZQ. 2001. Mutat Res. 477: 97-110. PMID: 11376691
6. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism.  |  Davidovic, L., et al. 2001. Exp Cell Res. 268: 7-13. PMID: 11461113
7. Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins.  |  Alemasova, EE. and Lavrik, OI. 2019. Nucleic Acids Res. 47: 3811-3827. PMID: 30799503
8. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B.  |  Darmon, AJ., et al. 1995. Nature. 377: 446-8. PMID: 7566124
9. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE.  |  Lazebnik, YA., et al. 1994. Nature. 371: 346-7. PMID: 8090205
10. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis.  |  Kaufmann, SH., et al. 1993. Cancer Res. 53: 3976-85. PMID: 8358726
11. PARP is important for genomic stability but dispensable in apoptosis.  |  Wang, ZQ., et al. 1997. Genes Dev. 11: 2347-58. PMID: 9308963
12. DNA repair: PARP - another guardian angel?  |  Jeggo, PA. 1998. Curr Biol. 8: R49-51. PMID: 9427640

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-PARP1 Antibody (F-2) has 893 citations in a variety of scientific publications.

Primary antibodies like Anti-PARP1 Antibody (F-2) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

PARP1 Antibody (F-2) Specifications

Alternate Product Name: PARP-1

Product Clone Name: F-2

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2a kappa light chain

Amino Acids: 764-1014

Epitope Target: PARP

Epitope Species: human

Product Reactivity/Detection: full-length PARP-1 and the C-terminal cleavage product of PARP-1

Species Reactivity/Detection: human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, IHC(P), ELISA

Vialing Information: Each vial contains 200 µg IgG_2a kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 893 citations in various scientific publications

Available Conjugates/Forms for PARP1 Antibody (F-2): AC: Agarose, AF405: Alexa Fluor^® 405, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin, TRITC: Rhodamine