BD Pharmingen™ Purified Mouse Anti-Human PARP

PARP

Mouse IgG1, κ

Human PARP

PARP [Poly(ADP-ribose) polymerase] is a 113 kDa nuclear chromatin-associated enzyme that catalyzes the transfer of ADP-ribose units from NAD+ to a variety of nuclear proteins including topoisomerases, histones, and PARP itself. The catalytic activity of PARP is increased in non-apoptotic cells following DNA damage, and PARP is thought to play an important role in mediating the normal cellular response to DNA damage. Additionally, PARP is a target of the caspase protease activity associated with apoptosis. During apoptosis, PARP is cleaved from a 113 kDa intact form into smaller 89 kDa and 24 kDa fragments. This process separates the amino-terminal DNA-binding domain of the enzyme from the carboxy-terminal catalytic domain resulting in the loss of normal PARP function. Although the role of PARP in apoptosis remains to be elucidated, PARP cleavage is considered to be a marker of apoptosis.  The 4C10-5 antibody recognizes both the intact 113 kDa form and 89 kDa fragment of PARP. The 4C10-5 antibody has been reported to recognize both native and denatured PARP. Purified human PARP was used as the immunogen and the antibody reported to react with an epitope located in the NAD binding domain.  In dot blot assays, the antibody reacts with the native enzyme in the presence or absence of bound DNA as well as after synthesis of covalently linked poly (ADP-ribose).  The 4C10-5 antibody is routinely tested by western blot analysis of untreated Jurkat T cells and Jurkat T cells induced to undergo apoptosis.

4C10-5 PARP [Poly(ADP-ribose) polymerase] is a 113 kDa nuclear chromatin-associated enzyme that catalyzes the transfer of ADP-ribose units from NAD+ to a variety of nuclear proteins including topoisomerases, histones, and PARP itself. The catalytic activity of PARP is increased in non-apoptotic cells following DNA damage, and PARP is thought to play an important role in mediating the normal cellular response to DNA damage. Additionally, PARP is a target of the caspase protease activity associated with apoptosis. During apoptosis, PARP is cleaved from a 113 kDa intact form into smaller 89 kDa and 24 kDa fragments. This process separates the amino-terminal DNA-binding domain of the enzyme from the carboxy-terminal catalytic domain resulting in the loss of normal PARP function. Although the role of PARP in apoptosis remains to be elucidated, PARP cleavage is considered to be a marker of apoptosis.  The 4C10-5 antibody recognizes both the intact 113 kDa form and 89 kDa fragment of PARP. The 4C10-5 antibody has been reported to recognize both native and denatured PARP. Purified human PARP was used as the immunogen and the antibody reported to react with an epitope located in the NAD binding domain.  In dot blot assays, the antibody reacts with the native enzyme in the presence or absence of bound DNA as well as after synthesis of covalently linked poly (ADP-ribose).  The 4C10-5 antibody is routinely tested by western blot analysis of untreated Jurkat T cells and Jurkat T cells induced to undergo apoptosis.

Mouse IgG1, κ

克隆 4C10-5 (RUO)

0.5 mg/ml

Western blot (Routinely Tested), Bioimaging (Tested During Development), Dot Blot, Flow cytometry, Immunoprecipitation (Reported)

Human (QC Testing)

PARP

Aqueous buffered solution containing ≤0.09% sodium azide.

研发参考(2) 1. Patel T, Gores GJ, Kaufmann SH. The role of proteases during apoptosis. FASEB J. 1996; 10(5):587-597. (Biology). 2. Ranjit GB, Cheng MF, Mackay W, Whitacre CM, Berger JS, Berger NA. Poly(adenosine diphosphoribose) polymerase in peripheral blood leukocytes from normal donors and patients with malignancies. Clin Cancer Res. 1995; 1(2):223-234. (Clone-specific: Flow cytometry, Western blot).