CNOT4 Antibody (343CT14.6.5): sc-517324

CNOT4 Antibody (343CT14.6.5) is a mouse monoclonal IgG2a kappa light chain antibody that detects CNOT4 protein of mouse, rat, and human origin by western blotting (WB) and immunoprecipitation (IP). Anti-CNOT4 antibody (343CT14.6.5) is available as a non-conjugated monoclonal isotype antibody. CNOT4, also known as CCR4-associated factor 4 and E3 ubiquitin-protein ligase CNOT4, plays a crucial role in the CCR4-NOT complex, which is essential for regulating gene expression and mRNA degradation. This complex is involved in various cellular processes, including the modulation of nuclear hormone receptor activities and the regulation of histone modifications, particularly Histone H3 lysine 4 methylation, through a ubiquitin-dependent pathway that likely engages the proteasome. CNOT4 consists of 575 amino acids and features a unique structural composition, including one C3H1-type zinc finger, one RING-type zinc finger, and one RNA recognition motif (RRM) domain. The presence of the RING domain facilitates CNOT4 binding to E2 ubiquitin ligases, enabling function as a UbcH5B-dependent ubiquitin-protein ligase (E3 ligase). CNOT4 undergoes alternative splicing, resulting in eight distinct isoforms, which may have diverse regulatory roles in cellular processes. Anti-CNOT4 antibody (343CT14.6.5) serves as an invaluable tool for researchers studying the intricate mechanisms of gene regulation and protein degradation pathways.

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CNOT4 Antibody (343CT14.6.5) References:

1. Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits.  |  Albert, TK., et al. 2000. Nucleic Acids Res. 28: 809-17. PMID: 10637334
2. The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers.  |  Hanzawa, H., et al. 2001. J Biol Chem. 276: 10185-90. PMID: 11087754
3. Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex.  |  Albert, TK., et al. 2002. EMBO J. 21: 355-64. PMID: 11823428
4. Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches.  |  Dominguez, C., et al. 2004. Structure. 12: 633-44. PMID: 15062086
5. Structure-based approaches to create new E2-E3 enzyme pairs.  |  Winkler, GS. and Timmers, HT. 2005. Methods Enzymol. 399: 355-66. PMID: 16338368
6. Modulation of Ubc4p/Ubc5p-mediated stress responses by the RING-finger-dependent ubiquitin-protein ligase Not4p in Saccharomyces cerevisiae.  |  Mulder, KW., et al. 2007. Genetics. 176: 181-92. PMID: 17513889
7. RING domains functioning as E3 ligases reveal distinct structural features: a molecular dynamics simulation study.  |  Zhao, JH., et al. 2008. J Biomol Struct Dyn. 26: 65-74. PMID: 18533727
8. Human Ccr4-Not complexes contain variable deadenylase subunits.  |  Lau, NC., et al. 2009. Biochem J. 422: 443-53. PMID: 19558367
9. CNOT4 enhances the efficacy of anti-PD-1 immunotherapy in a model of non-small cell lung cancer.  |  Zhang, B., et al. 2020. FEBS Open Bio. 10: 2631-2639. PMID: 33034149
10. The CNOT4 Subunit of the CCR4-NOT Complex is Involved in mRNA Degradation, Efficient DNA Damage Repair, and XY Chromosome Crossover during Male Germ Cell Meiosis.  |  Dai, XX., et al. 2021. Adv Sci (Weinh). 8: 2003636. PMID: 34026442
11. CNOT4 suppresses nonsmall cell lung cancer progression by promoting the degradation of PAF1.  |  Zhang, B., et al. 2023. Mol Carcinog. 62: 1563-1571. PMID: 37493105
12. Stalled translation by mitochondrial stress upregulates a CNOT4-ZNF598 ribosomal quality control pathway important for tissue homeostasis.  |  Geng, J., et al. 2024. Nat Commun. 15: 1637. PMID: 38388640