{"product_id":"recombinant-human-poly-adp-ribose-polymerase-1-parp1-partial-bhp10509805","title":"Recombinant Human Poly [ADP-ribose] polymerase 1 (PARP1), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eRecombinant Human Poly [ADP-ribose] polymerase 1 (PARP1), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Epigenetics and Nuclear Signaling research by enabling enzyme activity assays, kinetics\/structure–function studies and inhibitor or substrate screening in controlled in vitro settings.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 324-541aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression host can influence folding and the presence\/absence of post-translational modifications.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eTag \/ fusion:\u003c\/strong\u003e N-terminal 6xHis-GST-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular weight (reported):\u003c\/strong\u003e 55.2 kDa. Apparent size may vary with tags, processing, and gel conditions.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eWhen comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.\u003c\/p\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eThe gene commonly associated with this target is \u003cstrong\u003ePARP1\u003c\/strong\u003e. PARP1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt\/NCBI) and the recent literature for the specific organism and isoform.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eDissecting domain-specific functions of regulatory proteins involved in chromatin organization and transcriptional control.\u003c\/li\u003e \u003cli\u003eMapping protein–protein and protein–nucleic acid interactions that coordinate gene expression programs.\u003c\/li\u003e \u003cli\u003eBuilding in vitro assays for enzymatic activities and reader–writer–eraser mechanisms linked to epigenetic regulation.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e\u003cstrong\u003eRelevance:\u003c\/strong\u003e Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1\/TP53BP1, UIMC1\/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2\/TIP150. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and EEF1A1. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.\u003c\/p\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eEnzyme activity assays and kinetics measurements with defined substrates\/cofactors.\u003c\/li\u003e \u003cli\u003eInhibitor, activator, or substrate screening in biochemical assay formats.\u003c\/li\u003e \u003cli\u003eStructure–function analysis to interpret how sequence changes impact catalytic performance.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eIn quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative\/positive controls and, where possible, orthogonal assay formats that support the same conclusion.\u003c\/p\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eRecombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.\u003c\/li\u003e \u003cli\u003eTag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.\u003c\/li\u003e \u003cli\u003eSpecies and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.\u003c\/li\u003e \u003cli\u003eE. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProtKB entry for P09874 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P09874\/entry - NCBI Gene search (PARP1) — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=PARP1 - PubMed search (PARP1) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=PARP1 - RCSB PDB search (PARP1) — RCSB PDB — https:\/\/www.rcsb.org\/search?query=PARP1 - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53065301164397,"sku":"CSB-EP017457HU1-1MG","price":2062.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53065451340141,"sku":"CSB-EP017457HU1-100UG","price":480.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53065451372909,"sku":"CSB-EP017457HU1-20UG","price":256.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP017457HU1-SDS.jpg?v=1772476500","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-poly-adp-ribose-polymerase-1-parp1-partial-bhp10509805","provider":"BioHippo","version":"1.0","type":"link"}