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- Table of Contents
Facts about Poly [ADP-ribose] polymerase 2.
Mediates serine ADP-ribosylation of target proteins after interaction with HPF1; HPF1 conferring serine specificity (PubMed:28190768). .
Human | |
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Gene Name: | PARP2 |
Uniprot: | Q9UGN5 |
Entrez: | 10038 |
Belongs to: |
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No superfamily |
ADP-ribosyltransferase (NAD+; poly(ADP-ribose) polymerase)-like 2; ADPRT-2; ADPRT2pADPRT-2; ADPRTL2EC 2.4.2.30; ADPRTL3; hPARP-2; NAD(+) ADP-ribosyltransferase 2; PARP-2; poly (ADP-ribose) polymerase 2; poly (ADP-ribose) polymerase family, member 2; poly (ADP-ribosyl) transferase-like 2; poly [ADP-ribose] polymerase 2; poly(ADP-ribose) synthetase; Poly[ADP-ribose] synthase 2; poly[ADP-ribose] synthetase 2
Mass (kDA):
66.206 kDA
Human | |
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Location: | 14q11.2 |
Sequence: | 14; NC_000014.9 (20343041..20357904) |
Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus.
Nucleus.
Scientists can use PARP2 to aid with their research. By using it, they can test the protein's levels in various biological processes and to determine the levels of PARP2 in their specimens. Researchers can submit their results for product credits. This marker can aid scientists in understanding how PARP2 functions, whether they are working within a specific species or within cellular assays.
Boster Bio AntiPARP-2 Antibodies uses the PARP2 marker in order to identify protein levels within biological samples. The antibody binds one or more fusion proteins. The fusion proteins can be tagged with a fluorescent protein sequence or an antigenic-peptide sequence. This fusion protein can be recognized by an antibody by binding its peptide sub-substrat.
Boster Bio AntiPARP-2 Antibodies are available as a variety of formats. These kits come in both sterile and liquid formats. The reagents are safe to store at -20 degrees Celsius (80 degrees Fahrenheit), or in refrigerators at 40 degrees C for up a year. Prices vary depending on how long the immunogen is.
Poly(ADPribose polymerase-2) is an enzyme that plays an important role in the repair DNA damage. The enzyme plays a critical role in DNA repairs by transferring the ADP–D–ribosyl Group of NAD (+) to carboxyl groups. The enzyme recruits other repair factors to promote decompaction.
Cellular assays are a key tool in life science research, particularly in the preclinical stage of drug discovery. This method involves the cultivation of live cells in vitro as a model system to understand cell biochemistry and physiology. Cell culture assays are inexpensive and flexible and can be used to measure the behavior of cells or tissues. Cell culture assays have become more versatile thanks to emerging technologies like pluripotent stem cells.
The emerging technology of electric cell-substance impedance sensing can be used in drug discovery and screening. Its multiparameter capability allows for a better understanding cellular events. It can be used for drug discovery and to measure toxins. In fact, ECIS is used in a wide range of cellular studies. Here are a few examples.
A cell line called MCF7, or A549 is used to conduct this assay. The bioassay reagent, 3-(4,5-Dimethyl-2-thiazolyl)-2H-tetrazolium bromide, is used to detect the presence of specific bioactive compounds. The mechanism of inhibition of cell proliferation is determined by molecular docking analysis.
Fluorescently-labeled reporter probes can detect analyte and cell-cell interactions. Fluorescently labelled cells can be genetically modified so that they express intracellular luminescent substances. These assays are ideal for monitoring the effects of pathogens on intracellular functions. These technologies are made even more valuable by the use of fluorescent reporters in cell assays. They are also more cost-effective than radioactive probes.
There are many possible uses for the PARP2 marker in IFN Research. This is an mRNA–selective inhibitor virus-specificRNA that inhibits the replication a variety of viruses. The veev-based replicons contain full-length PARP7, PARP10, and PARP12L fusion proteins fused to a Flag tag at the amino termini.
PARP2 encodes a protein that inhibits cellular transcription. This protein is present in many tissues, and it plays a part in the prevention of HIV infection. The long isoform is responsible to inhibit cellular translation and ribosomemediated apoptosis. This protein is a crucial inhibitor of viral replication and can be used for the detection of disease-specific IFNs.
This gene is also used in research on immunoglobulin, which mediates cytokine production. PARP12L has an important role in antiviral function. PARP12L also forms multiple complexes with the cellular translation machinery. PARP2 marker in IFN research can be used to diagnose and treat patients with a variety infectious diseases.
Although IFN-induction is not required for PARP2, it's important to recognize that PARP inhibition may be an important factor in suppressing immune responses. PARP inhibition could be an effective adjuvant for other immunotherapeutic strategies. However more research is required to fully understand its mechanisms. Further research is needed in order to determine if PARP inhibition can reduce the development of different types of cancer.
PARP12L, however, has been shown to interact positively with ribosomes. This interaction is mediated through its amino-terminal region, which previously contained RNA-binding motif. These results indicate the importance and necessity of both PARP12Ldomains for rapid antiviral development. In conclusion, PARP12L-mCat and PARP12L-mAcc are effective inhibitors of VEEV/GFP/C1 virus replication.
Recent research used RAW264.7 cell lines to assess the role of PARP2 when IFN research was being conducted. The RAW264.7 cells were stimulated with LPS and IFNb for eight hours. After eight hours, cells were fixed and stained with endogenous PARP12.
Despite its role in DNA repair, PARP2 deficiency has been implicated in the development of several liver diseases, including cirrhosis and hepatitis. Although PARPs are the focus of many studies, their role is also important in signaling and gene expression regulation. PARPs are involved with DNA metabolism and architecture and regulate the activity of many proteins, including transcription factors, toposomerases, and transcription factors. PARP-2-deficient mice had cells that showed signs of base excision repair, XRCC1 activation, and delayed response to DNA strand break.
The protein is organised in the cell's nucleus. It interacts in the E domain with its surroundings by homodimerizing. The E domain of PARP-2 is responsible for homodimerization and acts as the protein/protein interface. PARP-2 contains a large number of glutamate residues. These are potential automodification sites. PARP-1 lacks these properties.
In mice, PARP2-/ mice make significantly fewer iNKT-cells than WT mice. Researchers examined the thymocyte populations to determine the mechanisms behind NKT-cell loss. PARP-2 deficient mice had lower numbers of mature T lymphocytes, and higher levels of immature cells. PARP-2 deficient mice also lacked wild-type maturation marker T lymphocyte markers.
The recruitment of other leukocyte populations is not affected by the absence of PARP2. Both genotypes recruit T lymphocytes, and B lymphocytes approximately 11 hours after ConA administration. NK cells and myeloid cell recruitment was also similar. CD69 was used to study T-lymphocytes.
PARP enzymes are responsible for detecting DNA damage. They act as DNA damage sensors by catalyzing the successive covalent addition of ADP-ribose units from NAD to a small set of nuclear acceptors. Furthermore, PARP enzymes can recruit scaffolding proteins to SSB lesions. PARP-1 might also help HR by recognizing and recruiting factors for DSB-related lesions.
PARP-1 & PARP-2 are two enzymes that can form poly(ADPribose), or (PARP-ribose), bonds. Both enzymes play an important role in the synthesis of DNA andRNA. They are involved in DNA replication and transcription. When these proteins fail to link, they fail to repair it. PARP-2 is essential for DNA repair and RNA synthesis, and a deficiency in mPARP-2 can cause this.
PMID: 10364231 by Ame J.-C., et al. PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.
PMID: 10329013 by Johansson M.; A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues.