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This POLR2A protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered. POLR2A encodes the largest subunit of RNA polymerase II that transcribes DNA into RNA. POLR2A regulates various biological processes, including transcription, cell cycle progression, and chromatin remodeling [1] [2] [3]. Mutations in POLR2A have been linked to specific types of tumors. Recurrent somatic POLR2A mutations have been identified in meningiomas [4]. POLR2A also promotes the proliferation of cancer cells such as in gastric cancer, by advancing cell cycle progression [5]. Furthermore, POLR2A has been found to interact with other proteins such as CREB1, to regulate transcription and cellular processes like osteoclastic bone resorption [6]. Studies have also shown that POLR2A positively regulates histone modifications such as H3K4me3, suggesting its role in establishing chromatin conformation and gene expression patterns [2]. Moreover, variations in the length of certain genetic markers, like the poly-T variant in SCAF4, can influence the binding of POLR2A and impact the transcription of nearby genes, potentially contributing to disease processes like amyotrophic lateral sclerosis [7]. References:[1] Y. Li, Y. Liu, H. Xu, G. Jiang, K. Jeught, Y. Fanget al., Heterozygous deletion of chromosome 17p renders prostate cancer vulnerable to inhibition of rna polymerase ii, Nature Communications, vol. 9, no. 1, 2018. https://doi.org/10.1038/s41467-018-06811-z[2] H. Yang, Z. Ma, P. Lin, C. Kuhn, M. Rahmeh, S. Mahneret al., Comparison of histone h3k4me3 between ivf and icsi technologies and between boy and girl offspring, International Journal of Molecular Sciences, vol. 22, no. 16, p. 8574, 2021. https://doi.org/10.3390/ijms22168574[3] 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. https://doi.org/10.3892/ol.2018.9508[4] V. Clark, A. Harmanc?, H. Bai, M. Youngblood, T. Lee, J. Baranoskiet al., Recurrent somatic mutations in polr2a define a distinct subset of meningiomas, Nature Genetics, vol. 48, no. 10, p. 1253-1259, 2016. https://doi.org/10.1038/ng.3651[5] Q. Jiang, J. Zhang, F. Li, X. Ma, F. Wu, J. Miaoet al., Polr2a promotes the proliferation of gastric cancer cells by advancing the overall cell cycle progression, Frontiers in Genetics, vol. 12, 2021. https://doi.org/10.3389/fgene.2021.688575[6] 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. https://doi.org/10.1002/jcp.30220[7] F. Theunissen, L. Flynn, R. Anderton, & P. Akkari, Short structural variants as informative genetic markers for als disease risk and progression, BMC Medicine, vol. 20, no. 1, 2022. https://doi.org/10.1186/s12916-021-02206-y
This POLR2A protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
POLR2A encodes the largest subunit of RNA polymerase II that transcribes DNA into RNA. POLR2A regulates various biological processes, including transcription, cell cycle progression, and chromatin remodeling [1] [2] [3]. Mutations in POLR2A have been linked to specific types of tumors. Recurrent somatic POLR2A mutations have been identified in meningiomas [4]. POLR2A also promotes the proliferation of cancer cells such as in gastric cancer, by advancing cell cycle progression [5].
Furthermore, POLR2A has been found to interact with other proteins such as CREB1, to regulate transcription and cellular processes like osteoclastic bone resorption [6]. Studies have also shown that POLR2A positively regulates histone modifications such as H3K4me3, suggesting its role in establishing chromatin conformation and gene expression patterns [2]. Moreover, variations in the length of certain genetic markers, like the poly-T variant in SCAF4, can influence the binding of POLR2A and impact the transcription of nearby genes, potentially contributing to disease processes like amyotrophic lateral sclerosis [7].
References:[1] Y. Li, Y. Liu, H. Xu, G. Jiang, K. Jeught, Y. Fanget al., Heterozygous deletion of chromosome 17p renders prostate cancer vulnerable to inhibition of rna polymerase ii, Nature Communications, vol. 9, no. 1, 2018. https://doi.org/10.1038/s41467-018-06811-z[2] H. Yang, Z. Ma, P. Lin, C. Kuhn, M. Rahmeh, S. Mahneret al., Comparison of histone h3k4me3 between ivf and icsi technologies and between boy and girl offspring, International Journal of Molecular Sciences, vol. 22, no. 16, p. 8574, 2021. https://doi.org/10.3390/ijms22168574[3] 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. https://doi.org/10.3892/ol.2018.9508[4] V. Clark, A. Harmanc?, H. Bai, M. Youngblood, T. Lee, J. Baranoskiet al., Recurrent somatic mutations in polr2a define a distinct subset of meningiomas, Nature Genetics, vol. 48, no. 10, p. 1253-1259, 2016. https://doi.org/10.1038/ng.3651[5] Q. Jiang, J. Zhang, F. Li, X. Ma, F. Wu, J. Miaoet al., Polr2a promotes the proliferation of gastric cancer cells by advancing the overall cell cycle progression, Frontiers in Genetics, vol. 12, 2021. https://doi.org/10.3389/fgene.2021.688575[6] 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. https://doi.org/10.1002/jcp.30220[7] F. Theunissen, L. Flynn, R. Anderton, & P. Akkari, Short structural variants as informative genetic markers for als disease risk and progression, BMC Medicine, vol. 20, no. 1, 2022. https://doi.org/10.1186/s12916-021-02206-y
| Cat.No | ACP23873 | Target Name | POLR2A |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Protein Length | Partial | Purity | >85% (SDS-PAGE) |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P24928 |
|---|
Uniprot Id
P24928
Target Species
Human
Target Name
POLR2A
Target Full Name
DNA-directed RNA polymerase II subunit RPB1
Target Function
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.
Target Subcellular Location
Nucleus. Cytoplasm. Chromosome.
Target Protein Families
RNA polymerase beta' chain family
Target Synonyms
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
Target Background
This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA.
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