p53R2 Antibody (H-3): sc-137173

p53R2 Antibody (H-3) is a mouse monoclonal IgG1 kappa light chain antibody, designed to target the p53R2 protein, also known as R2, of human origin. p53R2 monoclonal antibody (H-3) recognizes an epitope comprising amino acids 52-351 at the C-terminus of p53R2, ensuring precise and reliable binding for accurate detection in various assays. p53R2 is a critical subunit of ribonucleotide reductase, an enzyme essential for the synthesis of deoxyribonucleoside triphosphates (dNTPs) necessary for DNA repair and replication. Under normal cellular conditions, p53R2 is predominantly located in the cytoplasm, but in response to DNA damage, p53R2 translocates to the nucleus where p53R2 supplies dNTPs required for effective DNA repair mechanisms. This dynamic localization is vital for maintaining genomic stability and enabling cells to respond appropriately to genotoxic stress. Anti-p53R2 antibody (H-3) demonstrates broad species reactivity, effectively recognizing p53R2 from mouse, rat, and human origins across multiple applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). p53R2 (H-3) antibody is recommended for researchers studying cell cycle regulation, DNA synthesis, repair processes, and molecular pathways involved in tumor suppression. By facilitating reliable detection of p53R2, anti-p53R2 antibody (H-3) supports advancements in understanding p53R2′s role in cancer development and therapeutic responses. Whether employed in basic research or clinical studies, p53R2 monoclonal antibody (H-3) offers exceptional quality and performance to meet diverse experimental needs, making p53R2 (H-3) antibody a crucial reagent in molecular biology research.

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p53R2 Antibody (H-3) References:

1. p53R2 is a prognostic factor of melanoma and regulates proliferation and chemosensitivity of melanoma cells.  |  Matsushita, S., et al. 2012. J Dermatol Sci. 68: 19-24. PMID: 22902076
2. The roles of p53R2 in cancer progression based on the new function of mutant p53 and cytoplasmic p21.  |  Yousefi, B., et al. 2014. Life Sci. 99: 14-7. PMID: 24486301
3. Akt and p53R2, partners that dictate the progression and invasiveness of cancer.  |  Yousefi, B., et al. 2014. DNA Repair (Amst). 22: 24-9. PMID: 25086499
4. E2F1 regulates p53R2 gene expression in p53-deficient cells.  |  Qi, JJ., et al. 2015. Mol Cell Biochem. 399: 179-88. PMID: 25312903
5. Novel regulators and molecular mechanisms of p53R2 and its disease relevance.  |  Cho, EC. and Yen, Y. 2016. Biochimie. 123: 81-4. PMID: 26796884
6. p53R2 regulates thioredoxin reductase activity through interaction with TrxR2.  |  Park, SJ., et al. 2017. Biochem Biophys Res Commun. 482: 706-712. PMID: 27866984
7. p53R2 overexpression in cervical cancer promotes AKT signaling and EMT, and is correlated with tumor progression, metastasis and poor prognosis.  |  Jiang, C., et al. 2017. Cell Cycle. 16: 1673-1682. PMID: 28841361
8. p53R2 as a novel prognostic biomarker in nasopharyngeal carcinoma.  |  Chen, J., et al. 2017. BMC Cancer. 17: 846. PMID: 29237424
9. Effect of siRNA-mediated silencing of p53R2 gene on sensitivity of T-ALL cellsto Daunorubicin.  |  Kiani Ghalesardi, O., et al. 2023. Gene. 880: 147622. PMID: 37419428
10. Targeting CK2-mediated phosphorylation of p53R2 sensitizes BRCA-proficient cancer cells to PARP inhibitors.  |  Wang, C., et al. 2023. Oncogene. 42: 2971-2984. PMID: 37620447

The preferred R2 antibody is R2 Antibody (A-5): sc-398294.