Recombinant Human DNA-directed RNA polymerase II subunit RPB1 (POLR2A), partial

Code CSB-YP018327HU
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP018327HU
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP018327HU-B
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP018327HU
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP018327HU
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
DNA directed RNA polymerase II A; DNA-directed RNA polymerase II largest subunit RNA polymerase II 220 kd subunit; DNA-directed RNA polymerase II subunit A; DNA-directed RNA polymerase II subunit RPB1; DNA-directed RNA polymerase III largest subunit; hRPB220; hsRPB1; POLR2; Polr2a; POLRA; Polymerase (RNA) II (DNA directed) polypeptide A 220kDa; Polymerase (RNA) II (DNA directed) polypeptide A; RNA polymerase II subunit B1; RNA-directed RNA polymerase II subunit RPB1; RPB1; RPB1_HUMAN; RPBh1; RpIILS; RPO2; RPOL2
Homo sapiens (Human)
Protein Length
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Please contact us to get it.

POLR2A, the primary subunit of RNA polymerase II, plays a pivotal role in transcribing the majority of protein-coding genes [1]. It serves as a foundational element for transcription, mRNA processing, and chromosome remodeling [2]. Moreover, POLR2A codes for a critical component of the RNA polymerase II complex, essential for cell viability [3]. This protein is also implicated in various biological processes such as osteoporosis, nervous system functionality, and tumorigenesis [4]. Notably, POLR2A exhibits sensitivity to detrimental heterozygous variants altering its protein structure; its deficiency can lead to compromised global transcription and acceleration of cellular aging [5][6]. Intriguingly, cancer cells with only one functional copy of the POLR2A gene show heightened susceptibility to inhibition of its protein product, presenting a therapeutic opportunity [7]. Additionally, blocking POLR2A function leads to the inhibition of cancer cell growth [8]. Within the chromatin environment, POLR2A interacts with a spectrum of proteins including RPRD1A, RPRD1B, RPRD2, PCF11, and SCAF4 [9]. Furthermore, the degradation induced by α-amanitin results from its direct binding to POLR2A, triggering specific protein breakdown [10]. POLR2A is also implicated in transcription termination regulation through its interaction with SMN via its Tudor domain [11]. Lastly, inhibition of p-POLR2A-S2 by LDC067 influences the SIRT1-FOXO3-BNIP3 axis, enhancing therapeutic outcomes involving mitochondrial dysfunction in hepatocellular carcinoma [12].

[1] K. Yamada, M. Hayashi, H. Madokoro, H. Nishida, W. Du, K. Ohnumaet al., "Nuclear localization of cd26 induced by a humanized monoclonal antibody inhibits tumor cell growth by modulating of polr2a transcription", Plos One, vol. 8, no. 4, p. e62304, 2013.
[2] Y. Chai, F. Tan, S. Ye, F. Liu, & Q. Fan, "Identification of core genes and prediction of mirnas associated with osteoporosis using a bioinformatics approach", Oncology Letters, 2018.
[3] X. Han, D. Zhang, L. Ji, & X. Lu, "Anticancer opportunity created by loss of tumor suppressor genes", Technology in Cancer Research & Treatment, vol. 15, no. 6, p. 729-731, 2016.
[4] C. Liu, Y. Han, X. Zhao, B. Li, L. Xu, D. Liet al., "polr2a blocks osteoclastic bone resorption and protects against osteoporosis by interacting with creb1", Journal of Cellular Physiology, vol. 236, no. 7, p. 5134-5146, 2021.
[5] H. Haijes, M. Koster, H. Rehmann, D. Liu, H. Hákonarson, G. Cappuccioet al., "De novo heterozygous polr2a variants cause a neurodevelopmental syndrome with profound infantile-onset hypotonia", The American Journal of Human Genetics, vol. 105, no. 2, p. 283-301, 2019.
[6] S. Hou, D. Qu, Y. Li, B. Zhu, D. Liang, X. Weiet al., "Xab2 depletion induces intron retention in polr2a to impair global transcription and promote cellular senescence", Nucleic Acids Research, vol. 47, no. 15, p. 8239-8254, 2019.
[7] J. Eynden, S. Basu, & E. Larsson, "Somatic mutation patterns in hemizygous genomic regions unveil purifying selection during tumor evolution", Plos Genetics, vol. 12, no. 12, p. e1006506, 2016.
[8] M. Hayashi, H. Madokoro, K. Yamada, H. Nishida, C. Morimoto, M. Sakamotoet al., "Novel antibody-drug conjugate with anti-cd26 humanized monoclonal antibody and transcription factor iih (tfiih) inhibitor, triptolide, inhibits tumor growth via impairing mrna synthesis", Cancers, vol. 11, no. 8, p. 1138, 2019.
[9] M. Lavallée-Adam, J. Rousseau, C. Domecq, A. Bouchard, D. Forget, D. Faubertet al., "Discovery of cell compartment specific protein–protein interactions using affinity purification combined with tandem mass spectrometry", Journal of Proteome Research, vol. 12, no. 1, p. 272-281, 2012.
[10] K. Fluiter, A. Asbroek, M. Wissel, M. Jakobs, M. Wissenbach, H. Olssonet al., "In vivo tumor growth inhibition and biodistribution studies of locked nucleic acid (lna) antisense oligonucleotides", Nucleic Acids Research, vol. 31, no. 3, p. 953-962, 2003.
[11] Y. Li, A. Iqbal, W. Li, Z. Ni, D. Zhao, K. Abrahamet al., "A small molecule antagonist for the tudor domain of smn disrupts the interaction between smn and rnap ii",, 2019.
[12] J. Yao, J. Wang, Y. Xu, Q. Guo, Y. Sun, J. Liuet al., "Cdk9 inhibition blocks the initiation of pink1-prkn-mediated mitophagy by regulating the sirt1-foxo3-bnip3 axis and enhances the therapeutic effects involving mitochondrial dysfunction in hepatocellular carcinoma", Autophagy, vol. 18, no. 8, p. 1879-1897, 2021.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. 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 thought 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 site and is thought 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 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 levels of tha CTD-lysines. Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression.; (Microbial infection) Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.
Gene References into Functions
  1. XPC is an RNA polymerase II cofactor recruiting ATAC coactivator complex to promoters by interacting with E2F1. PMID: 29973595
  2. weak, multivalent interactions between TAF15 fibrils and heptads throughout RNA pol II CTD collectively mediate complex formation. PMID: 28945358
  3. This shows that CDK9 stimulates release of paused polymerase and activates transcription by increasing the number of transcribing polymerases and thus the amount of mRNA synthesized per time. PMID: 28994650
  4. Results identified rs2071504 in POLR2A gene to be associated with poor overall and disease-free survival of patients with an early-stage non-small cell lung cancer. PMID: 28922562
  5. Dara indicate that hydrogen peroxide alters RNA polymerase II (Pol II) occupancy at promoters and enhancers genome-wide. PMID: 28977633
  6. Rpb1/2 dynamics help govern the decision between sense and divergent antisense transcription. PMID: 28506463
  7. The results showed heterogeneity in the responses of individual KSHV episomes to stimuli within a single reactivating cell; those episomes that did respond to stimulation, aggregated within large domains that appear to function as viral transcription factories. A significant portion of cellular RNA polymerase II was trapped in these factories and served to transcribe viral genomes. PMID: 28331082
  8. Data show that inhibition of VCP/p97, or siRNA-mediated ablation of VCP/p97 impairs ultraviolet radiation (UVR)-induced RNA polymerase II (RNAPII) degradation. PMID: 28036256
  9. Role of chromatin-bound EGFR and ERK kinases in RNA polymerase 2 transcription PMID: 27587583
  10. recurrent somatic mutations in POLR2A hijack this essential enzyme and drive meningioma neoplasia PMID: 27548314
  11. the Elongin A ubiquitin ligase and the CSB protein function together in a common pathway in response to Pol II stalling and DNA damage PMID: 28292928
  12. By studying global gene expression patterns and genome-wide DNA-binding patterns of CGGBP1, it has been shown that a possible mechanism through which it affects the expression of RNA Pol II-transcribed genes in trans depends on Alu RNA. PMID: 25483050
  13. Using a 7,781-sample pan-cancer dataset, we first confirmed this in POLR2A are known to confer elevated sensitivity to pharmacological suppression.hese include the POLR2A interacting protein INTS10 as well as genes involved in mRNA splicing, nonsense-mediated mRNA PMID: 28027311
  14. HIV Tat precisely controls RNA polymerase II recruitment and pause release to fine-tune the initiation and elongation steps in target genes. PMID: 26488441
  15. TOP1 bound at promoters was discovered to become fully active only after pause-release. This transition coupled the phosphorylation of the carboxyl-terminal-domain (CTD) of RNA polymerase II (RNAPII) with stimulation of TOP1 above its basal rate, enhancing its processivity. PMID: 27058666
  16. Its variant is not related to sporadic PD in Chinese Han population. PMID: 26432391
  17. Data suggest RNA polymerase II (POLR2A) is extensively modified on its unique C-terminal domain (CTD) by O-GlcNAc transferase (OGT); efficient O-GlcNAcylation requires a minimum of 20 heptad CTD repeats in POLR2A and more than half of NTD of OGT. PMID: 26807597
  18. Serine phosphorylation stimulates whereas tyrosine phosphorylation inhibits the protein-binding activity of the RNA Pol II C-terminal domain. PMID: 26515650
  19. The amount of RNA polymerase II (RNAPII) on the HIV promoter and other viral regions was strongly diminished in HIV-infected CD4+ cells co-cultivated with cell non-cytotoxic antiviral response-expressing CD8+ cells. PMID: 26499373
  20. Ash2L acts in concert with P53 promoter occupancy to activate RNA Polymerase II by aiding formation of a stable transcription pre-initiation complex required for its activation. PMID: 25023704
  21. Data suggest that RNA polymerase II inhibitors may be a useful class of agent for targeting dormant leukaemia cells. PMID: 23767415
  22. This viral pre-initiation complex is composed of five different proteins in addition to Epstein-Barr virus BcRF1 and interacts with cellular RNA polymerase II PMID: 25165108
  23. Data show that E2F-1 form a complex with RNA polymerase II and protein PURA for transcriptional activation of the secondary promoter. PMID: 24819879
  24. human CD68 gene expression is associated with changes in Pol II phosphorylation and short-range intrachromosomal gene looping PMID: 17583472
  25. Authors show that the NSs protein of Schmallenberg virus (SBV) induces the degradation of the RPB1 subunit of RNA polymerase II and consequently inhibits global cellular protein synthesis and the antiviral response. PMID: 24828331
  26. This study reveals that TCERG1 regulates HIV-1 transcriptional elongation by increasing the elongation rate of RNAPII and phosphorylation of Ser 2 within the carboxyl-terminal domain. PMID: 24165037
  27. Slow Pol II elongation allows weak splice sites to be recognized, leading to higher inclusion of alternative exons. PMID: 24793692
  28. sequence-specific double strand DNA breaks are sufficient to activate the positive transcription elongation factor b (P-TEFb), to trigger hyperphosphorylation of the largest RNA polymerase II carboxyl-terminal-domain (Rpb1-CTD) and to induce activation of p53-transcriptional axis resulting in cell cycle arrest. PMID: 23906511
  29. interaction with nuclear CD26 and POLR2A gene PMID: 23638030
  30. RECQL5 contacts the Rpb1 jaw domain of Pol II at a site that overlaps with the binding site for the transcription elongation factor TFIIS. Binding of RECQL5 to Pol II interferes with the ability of TFIIS to promote transcriptional read-through in vitro. PMID: 23748380
  31. Data show that p68/DdX5 immunoprecipitated with RNA polymerase II (RNAP II) and suggest p68 is important in facilitating beta-catenin and androgen receptor (AR) transcriptional activity in prostate cancer cells. PMID: 23349811
  32. inhibition of the transition of paused RNA PolII to productive elongation, described here for p21(CIP1), is a general mechanism by which transcription factor Sp3 fine-tunes gene expression. PMID: 23401853
  33. RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. PMID: 23395899
  34. Data indicate that polyamide treatment activates p53 signaling and results in a time- and and dose-dependent depletion of the RNA polymerase II (RNAP2) large subunit RPB1. PMID: 23319609
  35. CTCF binding sites regulate mRNA production, RNA polymerase II (RNAPII) programming, and nucleosome organization of the Kaposi's sarcoma-associated herpesvirus latency transcript control region. PMID: 23192870
  36. site-specific p65 phosphorylation targets NF-kappaB activity to particular gene subsets on a global level by influencing p65 and p-RNAP II promoter recruitment PMID: 23100252
  37. BRD4-driven Pol II phosphorylation at serine 2 plays an important role in regulating lineage-specific gene transcription in human CD4+ T cells. PMID: 23086925
  38. SNAPC1 is a general transcriptional coactivator that functions through elongating RNAPII. PMID: 22966203
  39. Cyclin K1 is the primary cyclin partner for CDK12/CrkRS and it is required for activation of CDK12/CrkRS to phosphorylate the C-terminal domain of RNA Pol II. PMID: 22988298
  40. Studies indicate that the super elongation complex (SEC) consisting of ELL, P-TEFb (CDK9) and MLL required for rapid transcriptional induction in the presence or absence of paused RNA polymerase II (Pol II). PMID: 22895430
  41. Results indicate roles for both the RNA polymerase II C-terminal domain (CTD) and O-GlcNAc in the regulation of transcription initiation. PMID: 22605332
  42. Here, the authors report phosphorylation of Thr4 by Polo-like kinase 3 in mammalian cells. PMID: 22549466
  43. Studies suggest activator-induced structural shifts within Mediator trigger activation of stalled Pol II. PMID: 21326907
  44. These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly. PMID: 22343046
  45. evidence that phosphorylation of Rpb1 CTD Thr4 residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes PMID: 22053051
  46. Parcs/Gpn3 plays a critical role in the nuclear accumulation of RNAP II, and this function explains the relative importance of Parcs/Gpn3 in cell proliferation. PMID: 21782856
  47. kinetics of RNA polymerase II elongation during co-transcriptional splicing PMID: 21264352
  48. Data show that MicroRNA promoter identification based upon RPol II binding patterns provides important temporal and spatial measurements regarding the initiation of transcription. PMID: 21072189
  49. The deregulation of cellular NIPP1/PP1 holoenzyme affects RNAPII phosphorylation and pointing to NIPP1 as a potential regulatory factor in RNAPII-mediated transcription. PMID: 20941529
  50. Elevated PHD1 concomitant with decreased PHD2 are causatively related to Rpb1 hydroxylation and oncogenesis in human renal clear cell carcinomas with WT VHL gene. PMID: 20978146

Show More

Hide All

Subcellular Location
Nucleus. Cytoplasm. Chromosome.
Protein Families
RNA polymerase beta' chain family
Database Links

HGNC: 9187

OMIM: 180660

KEGG: hsa:5430

STRING: 9606.ENSP00000314949

UniGene: Hs.270017

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1