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50T
| 产品编号 | IHC0626M |
| 英文名称 | Mouse Phospho-POLR2A (Ser5) Ready-To-Use IHC Kit |
| 中文名称 | 小鼠磷酸化RNA聚合酶II CTD即用型免疫组化试剂盒 |
| 英文别名 | 220kDa; hRPB220; hsRPB1; POLR2; POLR2A; POLRA; RPB1; RPBh1; Rpii215; RpIILS; RPO2; Rpo2-1; RPOL2 |
| 产品应用 | IHC-P Not yet tested in other applications. |
| 交叉反应 | Mouse |
| 亚基 | Component of the RNA polymerase II (Pol II) core complex consisting of 12 subunits: a ten-subunit catalytic core composed of POLR2A/RPB1, POLR2B/RPB2, POLR2C/RPB3, POLR2I/RPB9, POLR2J/RPB11, POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5 and a mobile stalk composed of two subunits POLR2D/RPB4 and POLR2G/RPB7, protruding from the core and functioning primarily in transcription initiation. Part of Pol II(G) complex, in which Pol II core associates with an additional subunit POLR2M; unlike conventional Pol II, Pol II(G) functions as a transcriptional repressor. Part of TBP-based Pol II pre-initiation complex (PIC), in which Pol II core assembles with general transcription factors and other specific initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex mediates DNA unwinding and targets Pol II core to the transcription start site where the first phosphodiester bond forms (PubMed:27193682, PubMed:30190596, PubMed:9852112). Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, Pol II, SUPT5H, and NCL/nucleolin (PubMed:10393184, PubMed:10454543, PubMed:17234882). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (PubMed:28076779). Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA and may couple transcription to pre-mRNA splicing (PubMed:21536736). Interacts (via the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes (PubMed:26700805). Interacts via the phosphorylated C-terminal domain with WDR82 and with SETD1A and SETD1B only in the presence of WDR82 (PubMed:17998332). When phosphorylated at 'Ser-5', interacts with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2' does not interact (PubMed:14992727). When phosphorylated at 'Ser-5', interacts with ZMYND8; the form phosphorylated at 'Ser-2' does not interact (PubMed:26700805). When phosphorylated at 'Ser-2', interacts with SUPT6H (via SH2 domain) (PubMed:17234882). Interacts with RECQL5 and TCEA1; binding of RECQL5 prevents TCEA1 binding (PubMed:20231364, PubMed:23748380). The phosphorylated C-terminal domain interacts with FNBP3 (PubMed:12381297). The phosphorylated C-terminal domain interacts with SYNCRIP (PubMed:12376575). Interacts with ATF7IP (PubMed:19106100). Interacts with DDX5 (PubMed:12527917). Interacts with WWP2 (By similarity). Interacts with SETX (PubMed:23149945, PubMed:26700805). Interacts (phosphorylated) with PIH1D1 (PubMed:24656813). Interacts (via the C-terminal domain (CTD)) with TDRD3 (PubMed:26700805). Interacts with PRMT5 (PubMed:26700805). Interacts with XRN2 (PubMed:26700805). Interacts with SAFB/SAFB1 (PubMed:9671816). Interacts with CCNL1 (Probable). Interacts with CCNL2 (PubMed:14684736). Interacts with MYO1C (By similarity). Interacts with PAF1 (PubMed:16491129). Interacts with SFRS19 (PubMed:15992770). Interacts (via C-terminus) with CMTR1 (PubMed:18533109). Interacts (via C-terminus) with CTDSP1 (PubMed:17157258). Interacts (via C-terminus) with SCAF8 (PubMed:18550522). Interacts (via the C-terminal domain (CTD)) with CCNT2 (PubMed:15563843). Interacts with FUS (PubMed:26124092). Interacts with MCM3AP isoform GANP (PubMed:23652018). Interacts with kinase SRPK2; the interaction occurs during the co-transcriptional formation of inappropriate R-loops (PubMed:28076779). Interacts with SETD2 (PubMed:16118227, PubMed:16314571). Interacts with UVSSA (PubMed:32142649). Interacts with ERCC6 (PubMed:32142649). Interacts with the TFIIH complex (PubMed:32142649). Interacts (via the C-terminal domain) with IVNS1ABP (via Kelch repeats) (PubMed:30538201).By Similarity33 PublicationsCurated (Microbial infection) Interacts with herpes simplex virus 1 protein ICP22; this interaction causes loss of CTD 'Ser-2' phosphorylation from Pol II engaged in transcription (PubMed:23029222). |
| 亚细胞定位 | #Chromosome #Cytoplasm #DNA-directed RNA polymerase #Nucleus |
| 翻译后修饰 | The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated (PubMed:17234882, PubMed:19450536, PubMed:19667075, PubMed:19136461, PubMed:26566685, PubMed:28076779, PubMed:32142654, PubMed:33243860, PubMed:34004147). The phosphorylation activates Pol II (PubMed:33243860). Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9 (PubMed:19450536, PubMed:19667075, PubMed:19136461, PubMed:21127351). POLR2A associated with DNA is specifically phosphorylated at 'Ser-5' of the CTD by CDK7, promoting transcription initiation by triggering dissociation from DNA (PubMed:19136461, PubMed:26257281, PubMed:28768201). Phosphorylated at 'Ser-2', Ser-5' and 'Ser-7' of the CTD by CDK9 (P-TEFb complex), promoting transcription elongation (PubMed:19667075, PubMed:21127351). Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts (PubMed:22137580). The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed (PubMed:19450536, PubMed:19667075, PubMed:19136461, PubMed:33243860, PubMed:34004147). Dephosphorylated by the INTAC complex when transcripts are unfavorably configured for transcriptional elongation, leading to premature transcription termination: dephosphorylation is mediated by the PPP2CA component of the INTAC complex (PubMed:33243860, PubMed:34004147, PubMed:37080207). In response to replication stress, dephosphorylated at 'Ser-5' of the CTD by the PNUTS-PP1 complex, promoting RNA polymerase II degradation (PubMed:33264625). Dephosphorylated by the protein phosphatase CTDSP1 (PubMed:17157258). Dephosphorylated at 'Ser-2' following UV irradiation Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. Regulates initiation or early elongation steps of transcription specially for inducible genes. Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD. Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated by the DCX(ERCC8) complex (also named CSA complex) on Lys-1268 at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery (PubMed:22466610, PubMed:32142649, PubMed:32142654, PubMed:34526721, PubMed:35633597). At stalled RNA pol II where TC-NER has failed, RBX1-mediated polybiquitination at Lys-1268 may lead to proteasome-mediated degradation in a UBAP2- and UBAP2L-dependent manner; presumably to halt global transcription and enable 'last resort' DNA repair pathways (PubMed:35633597). Ubiquitinated by the BCR(ARMC5) complex when transcripts are unfavorably configured for transcriptional elongation: the BCR(ARMC5) complex specifically catalyzes ubiquitination of POLR2A phosphorylated at 'Ser-5' of the C-terminal domain (CTD), leading to POLR2A degradation (PubMed:35687106, PubMed:39504960, PubMed:39667934). Ubiquitination by the BCR(ARMC5) complex takes place at residues distinct from Lys-1268 (PubMed:39667934). Ubiquitinated by WWP2 leading to proteasomal degradation (By similarity) |
| 相似性 | Belongs to the RNA polymerase beta' chain family. |
| 功能 | Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:28108474, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg2+-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg2+ ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg2+ ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:8381534, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534). Through its unique C-terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA (By similarity) (PubMed:24207025, PubMed:26124092). RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription. (Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicase and transcriptase for the viral RNA circular genome. |
| 保存条件 | Please store components at the temperatures indicated on the individual tube labels. The kit is stable for 6 months from the date of receipt. |
| 背景资料 | DNA-directed RNA polymerase II subunit RPB1 (POLR1A) is a DNA-dependent RNA polymerase that catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. POLR1A is the largest subunit and is a catalytic component of RNA polymerase II which synthesizes mRNA precurors and many functional non-coding RNAs. It also forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft, and the jaws that are though to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic stie and is through to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II's largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination, and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levelts of the CTD-lysines. |
| 应用 | 推荐稀释比例 |
Immunohistochemical analysis of paraffin embedded Mouse colon tissue slide using IHC0626M (Mouse Phospho-POLR2A (Ser5) Kit).
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Mouse Phospho-POLR2A (Ser5) Ready-To-Use IHC Kit(IHC0626M)-50T
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