emerin Antibody (G-10): sc-398067

emerin Antibody (G-10) is a mouse monoclonal IgG2b antibody that detects emerin in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Emerin is a crucial component of the nuclear lamina, playing a significant role in maintaining the structural integrity of the nuclear envelope and facilitating chromatin organization. Emerin′s localization to the nuclear membrane is vital for proper nuclear function, as emerin helps anchor the nuclear lamina to the inner nuclear membrane, thereby influencing gene expression and cellular signaling pathways. Mutations in the gene encoding emerin can lead to the X-linked recessive disorder Emery-Dreyfuss muscular dystrophy (EDMD), which manifests as progressive muscle weakness, contractures, and cardiac issues. Lack of emerin disrupts the normal association between the nuclear membrane and the lamina, contributing to the pathophysiology of EDMD. Emerin′s specific localization to desmosomes and fasciae adherentes in cardiac tissue may explain the conduction defects observed in affected patients, highlighting emerin′s critical role in both muscle and cardiac health. anti-emerin antibody (G-10) is an essential tool for researchers investigating the molecular mechanisms underlying EDMD and related disorders.

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emerin Antibody (G-10) References:

1. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy.  |  Haraguchi, T., et al. 2004. Eur J Biochem. 271: 1035-45. PMID: 15009215
2. Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3.  |  Leach, N., et al. 2007. J Virol. 81: 10792-803. PMID: 17652388
3. Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties.  |  Herrada, I., et al. 2015. ACS Chem Biol. 10: 2733-42. PMID: 26415001
4. MAPK signaling pathways and HDAC3 activity are disrupted during differentiation of emerin-null myogenic progenitor cells.  |  Collins, CM., et al. 2017. Dis Model Mech. 10: 385-397. PMID: 28188262
5. Expression Profiling of Differentiating Emerin-Null Myogenic Progenitor Identifies Molecular Pathways Implicated in Their Impaired Differentiation.  |  Iyer, A., et al. 2017. Cells. 6: PMID: 29065506
6. RanGTPase regulates the interaction between the inner nuclear membrane proteins, Samp1 and Emerin.  |  Vijayaraghavan, B., et al. 2018. Biochim Biophys Acta Biomembr. 1860: 1326-1334. PMID: 29510091
7. Emerin modulates spatial organization of chromosome territories in cells on softer matrices.  |  Pradhan, R., et al. 2018. Nucleic Acids Res. 46: 5561-5586. PMID: 29684168
8. Role of the nuclear membrane protein Emerin in front-rear polarity of the nucleus.  |  Nastały, P., et al. 2020. Nat Commun. 11: 2122. PMID: 32358486
9. A novel mutation in human EMD gene and mitochondrial dysfunction in emerin knockdown cardiomyocytes.  |  Du, Z., et al. 2022. J Cell Mol Med. 26: 5054-5066. PMID: 36106556
10. Distribution of emerin and lamins in the heart and implications for Emery-Dreifuss muscular dystrophy.  |  Manilal, S., et al. 1999. Hum Mol Genet. 8: 353-9. PMID: 9949197

The preferred emerin antibody is emerin Antibody (H-12): sc-25284.