PARP2 Human

Poly (ADP-Ribose) Polymerase 2 Human Recombinant
Cat. No.
BT2830
Source
Escherichia Coli.
Synonyms
ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PARP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (233-583a.a) and having a molecular mass of 42.5kDa. PARP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Poly (ADP-Ribose) Polymerase 2 (PARP2) is an enzyme that plays a role in DNA repair. It catalyzes the addition of ADP-ribose units to proteins. Unlike PARP1, PARP2 lacks a DNA binding domain. However, it possesses a catalytic domain similar to PARP1. While PARP2 can catalyze poly (ADP-ribosyl)ation, its N-terminal region might contribute to its localization within the nucleus and/or nucleolus. Two different isoforms of PARP2 are produced due to alternative splicing.
Description
Recombinant human PARP2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 376 amino acids (233-583a.a), resulting in a molecular weight of 42.5 kDa. A 25 amino acid His-tag is fused to the N-terminus of PARP2. The protein undergoes purification using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The provided PARP2 solution has a concentration of 1mg/ml. It is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.4M urea, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), keep the PARP2 vial refrigerated at 4°C. For extended storage, freeze the vial at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of PARP2 is greater than 85%, as determined by SDS-PAGE analysis.
Synonyms
ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQLDLR VQELIKLICN VQAMEEMMME MKYNTKKAPL GKLTVAQIKA GYQSLKKIED CIRAGQHGRA LMEACNEFYT RIPHDFGLRT PPLIRTQKEL SEKIQLLEAL GDIEIAIKLV KTELQSPEHP LDQHYRNLHC ALRPLDHESY EFKVISQYLQ STHAPTHSDY TMTLLDLFEV EKDGEKEAFR EDLHNRMLLW HGSRMSNWVG ILSHGLRIAP PEAPITGYMF GKGIYFADMS SKSANYCFAS RLKNTGLLLL SEVALGQCNE LLEANPKAEG LLQGKHSTKG LGKMAPSSAH FVTLNGSTVP LGPASDTGIL NPDGYTLNYN EYIVYNPNQV RMRYLLKVQF NFLQLW.

Product Science Overview

Discovery and Function

PARP-2 was initially identified in connection with DNA repair mechanisms. It is involved in the base excision repair (BER) pathway, a critical process for repairing single-strand breaks in DNA . PARP-2 catalyzes the transfer of ADP-ribose units from NAD+ to target proteins, a process known as poly (ADP-ribosyl)ation . This modification is essential for recruiting and activating other proteins involved in DNA repair.

Physiological and Pathophysiological Roles

PARP-2 has been implicated in several physiological and pathophysiological processes, including:

  • Genome Maintenance: It helps protect centromeres and telomeres, ensuring proper chromosome segregation during cell division .
  • Spermiogenesis and Thymopoiesis: PARP-2 is involved in the development of sperm cells and thymocytes .
  • Inflammation and Metabolism: Recent studies have shown that PARP-2 influences gene expression related to inflammation and metabolism. It interacts with PPARγ and SIRT1, affecting mitochondrial activity and insulin sensitivity .
Recombinant PARP-2

Human recombinant PARP-2 is produced using recombinant DNA technology, which involves inserting the PARP-2 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes.

Research and Therapeutic Potential

PARP-2 has gained significant attention in the field of cancer research. Inhibitors targeting PARP enzymes, including PARP-2, have shown promise in treating cancers with defects in DNA repair pathways, such as BRCA1/2-mutated breast and ovarian cancers . These inhibitors work by exploiting the concept of synthetic lethality, where the inhibition of PARP activity leads to the accumulation of DNA damage and cell death in cancer cells deficient in other DNA repair mechanisms.

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