PARP2 (human, recombinant)

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Cat No: 32562

Proteins - Enzymes

Poly(ADP-Ribose) polymerase 2 (PARP2) is an ADP-ribosylating enzyme with a role in the DNA damage response (DRR).{61141,61142} It is composed of a natively disordered N-terminal region containing a nuclear localization sequence, a central Trp-Gly-Arg ...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

PARP 2 1 ADPRibose ribosyl transferase polyribosylation osteo sarcoma ARTD ADPRT ADPRTL 2

Product Overview:
Poly(ADP-Ribose) polymerase 2 (PARP2) is an ADP-ribosylating enzyme with a role in the DNA damage response (DRR).{61141,61142} It is composed of a natively disordered N-terminal region containing a nuclear localization sequence, a central Trp-Gly-Arg (WGR) domain that is essential to DNA damage-dependent catalytic domain activity, and a C-terminal catalytic domain (CAT) that contains an ADP-ribosyltransferase fold and a regulatory helical subdomain.{61142} PARP2 is ubiquitously expressed and localized to the nucleus where it is preferentially activated by the presence of PARP1-induced poly(ADP)-ribosylation (PARylation) induced by PARP1 (Item No. 32561) at sites of single-stranded DNA breaks. The WGR domain binds directly to DNA and activates PAR catalytic activity and branched PAR chain synthesis through cross-talk with the helical subdomain.{61141,61142} PARP2 PARylates itself and other proteins, including transcription factors, influencing multiple biological processes, such as transcription, genome maintenance, and cell signaling.{61143} PARP2 expression is negatively correlated with the amount of tumor immune infiltrate in tumor samples isolated from patients with osteosarcoma.{61144} Cayman’s PARP2 (human, recombinant) protein can be used for enzyme assay applications. This protein consists of 582 amino acids and has a calculated molecular weight of 95.5 kDa.

Size	10 µg
Shipping	dry ice
Host	Insect cells
Formulation	40 mM Tris-HCl, pH 8.0, with 110 mM sodium chloride, 2.2 mM potassium chloride, 16 mM glutathione, 20% glycerol, and 3 mM DTT
Purity	≥50% estimated by SDS-PAGE
Custom Code	3504.00
UNSPSC code	12352204

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.