POLR2A Antibodies

Structure of POLR2A

POLR2A is a large protein molecule with a molecular weight of approximately 217 kDa. Its size varies slightly among different species due to differences in domain structures.

POLR2A contains approximately 1970 amino acids and is the largest subunit of RNA polymerase II. Its protein structure consists of an N-terminal domain, a core catalytic domain, and a unique C-terminal domain. The C-terminal domain contains multiple Tyr-Ser-Pro-Thr-Ser-Pro-Ser heptapeptide repeat sequences, serving as a transcriptional regulatory platform that can be phosphorylated. This subunit, together with the other 11 subunits, constitutes the full enzyme of RNA polymerase II. During transcription, it is responsible for catalyzing the synthesis of RNA chains and interacts with various transcription factors.

Fig. 1 circMETTL6 Suppresses Ovarian Cancer by Destabilizing POLR2A.¹

Key structural characteristics of POLR2A:

• Contains a core catalytic region composed of multiple domains
• Has a unique C-terminal domain, consisting of 52 heptapeptide repeat sequences
• The C-terminal domain can be phosphorylated and serves as a transcriptional regulatory platform
• Assembles with other 11 subunits to form a complete RNA polymerase II complex

Functions of POLR2A

The core function of POLR2A is to act as the largest subunit of RNA polymerase II, responsible for catalyzing the conversion of DNA into RNA. However, it also plays a crucial role in various cellular processes, including regulating gene expression and participating in cellular stress responses.

Unlike the cooperative binding curve of hemoglobin, as the core scaffold of the transcriptional complex, the expression level and phosphorylation status of POLR2A directly affect the overall transcriptional activity, demonstrating its central role in gene expression regulation.

Applications of POLR2A and POLR2A Antibody in Literature

1. Yu, Mengqian, et al. "CircMETTL6 Suppresses Ovarian Cancer Cell Growth and Metastasis Through Inhibition of GDF15 Transcription by Disrupting the NONO‐POLR2A Complex." Advanced Science 12.12 (2025): 2411717. https://doi.org/10.1002/advs.202411717

The article indicates that in ovarian cancer, the expression of circMETTL6 is downregulated and is associated with poor prognosis. Overexpression of circMETTL6 can bind to NONO, disrupt the binding of NONO to POLR2A, leading to instability of POLR2A, and subsequently inhibiting the transcription of GDF15 and the malignant progression of the tumor. This study reveals the key tumor-suppressing mechanism of the circMETTL6/NONO/POLR2A axis.

2. Zhang, Diekuo, et al. "USP10 inhibits ferroptosis via deubiquinating POLR2A in head and neck squamous cell carcinoma." Advanced Science 12.36 (2025): e12271. https://doi.org/10.1002/advs.202412271

The article indicates that in head and neck squamous cell carcinoma, the high expression of USP10 is associated with poor prognosis. USP10 stabilizes POLR2A through deubiquitination, thereby transcriptionally activating SLC7A11, and thereby inhibiting ferroptosis. Targeting USP10 can enhance the response of cancer cells to ferroptosis inducers. This study reveals the key regulatory mechanism of the USP10/POLR2A/SLC7A11 axis.

3. Jiang, Qiuyu, et al. "POLR2A promotes the proliferation of gastric cancer cells by advancing the overall cell cycle progression." Frontiers in genetics 12 (2021): 688575. https://doi.org/10.3389/fgene.2021.688575

The article indicates that POLR2A is highly expressed in gastric cancer and is closely related to tumor progression. POLR2A accelerates the cell cycle process by comprehensively promoting the transcription of cyclins and CDKs, while inhibiting cell apoptosis and promoting migration, thereby exerting a carcinogenic effect. This study reveals the carcinogenic mechanism of POLR2A in gastric cancer.

4. Hou, Shuai, et al. "XAB2 depletion induces intron retention in POLR2A to impair global transcription and promote cellular senescence." Nucleic Acids Research 47.15 (2019): 8239-8254. https://doi.org/10.1093/nar/gkz532

The article indicates that the absence of XAB2 leads to splicing defects and intron retention in POLR2A, resulting in a significant decrease in its RNA and protein levels, and subsequently inhibiting global transcription. The upregulated Dom34 can mediate the degradation of POLR2A mRNA. XAB2 maintains POLR2A expression by interacting with SNW1 through the TPR motif, antagonizing cellular aging. This study reveals the regulatory mechanism of the XAB2/POLR2A axis.

5. Mao, Chun‐guo, et al. "BCAR1 promotes proliferation and cell growth in lung adenocarcinoma via upregulation of POLR2A." Thoracic cancer 11.11 (2020): 3326-3336. https://doi.org/10.1111/1759-7714.13676

The article indicates that in lung adenocarcinoma, BCAR1 plays a role in carcinogenesis by promoting proliferation and colony formation. Mechanistically, BCAR1 is positively correlated with the expression of POLR2A, and knocking out BCAR1 can down-regulate POLR2A. Clinical data show that the co-high expression of both is associated with poor prognosis. Studies have suggested that BCAR1 may promote tumor progression by up-regulating POLR2A.

Creative Biolabs: POLR2A Antibodies for Research

Creative Biolabs specializes in the production of high-quality POLR2A antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom POLR2A Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our POLR2A antibodies, custom preparations, or technical support, contact us at email.