PARP2 Protein
Quick Overview for PARP2 Protein (ABIN925019)
Target
See all PARP2 ProteinsProtein Type
Origin
Source
Purity
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Characteristics
- 380 units/mg (one unit synthesizes 1 nmole of poly(ADP-ribose) per min at 25°C, pH 7.5.
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Purification
- Affinity purified
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Poly (ADP-Ribose) Polymerase 2 (PARP2) (AA 1-559) protein (His tag)
custom-made PARP2 Origin: Mouse Host: HEK-293 Cells Recombinant > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
Poly (ADP-Ribose) Polymerase 2 (PARP2) (AA 1-583) protein (His tag)custom-made PARP2 Origin: Human Host: HEK-293 Cells Recombinant > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
Poly (ADP-Ribose) Polymerase 2 (PARP2) (AA 430-583) protein (His-IF2DI Tag)PARP2 Origin: Human Host: Escherichia coli (E. coli) Recombinant Greater than 90 % as determined by SDS-PAGE. ELISA, WB
Poly (ADP-Ribose) Polymerase 2 (PARP2) (AA 435-534) protein (GST tag)PARP2 Origin: Human Host: Wheat germ Recombinant ELISA, WB, AP, AA
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Restrictions
- For Research Use only
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Format
- Liquid
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Storage
- -80 °C
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- PARP2 (Poly (ADP-Ribose) Polymerase 2 (PARP2))
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Alternative Name
- PARP-2
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Background
- The cDNA encoding human poly(ADP-ribose) polymerase (PARP) was cloned by several groups simultaneously. With the discovery of new members (homologs) of the PARP family, PARP is newly referred to as PARP-1. The isolated cDNAs from mouse and human encode a protein with considerable homology to the catalytic domain of PARP-1. This protein, termed PARP-2, is a 64 kDa protein that contains a nuclear localization signal (NLS) and is activated by DNA breaks, although its DNA- binding domain is very different from that of PARP-1. In recent years evidence has accumulated that poly(ADP-ribose) polymerase (PARP) plays a role in DNA repair and a substantial effort has been invested to elucidate the physiological function of the PARP pathway in cellular recovery from DNA damage. PARP has been found in the base excision repair (BER) complex with DNA polymerase-, ligase III and x-ray repair cross-complementing 1 (XRCC1). PARP- 1 and PARP-2, even though lacking the zinc- finger domains, bind to single and double strand breaks during oxidative stress. In general, it appears that an early enzymatic activation of PARP occurs upon DNA-strand break formation. Binding of PARP to a DNA nick may then cause a transient halt to cellular activity and protect the DNA from sister chromatid associated proteins such as histones. Nicotinamide is cleaved in this step from the substrate NAD+ by PARP and the so synthesized poly(ADP)-ribose (PAR) is then used to generate ATP. Specific
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Pathways
- DNA Damage Repair
Target
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