Obscurin Antibody (5C20): sc-517125

Obscurin Antibody (5C20) is a mouse monoclonal IgG2a kappa light chain antibody that detects Obscurin protein of human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-Obscurin antibody (5C20) is available as a non-conjugated isotype antibody. Obscurin, a member of the protein kinase superfamily, is a large protein consisting of 7968 amino acids, predominantly expressed in skeletal and cardiac muscle tissues. Obscurin plays a crucial role in maintaining sarcomere structural integrity, specifically localized near the M-band and Z-disk, where Obscurin is involved in G-protein regulated pathways that facilitate new myofibril formation. Notably, Obscurin contains 55 immunoglobulin-like domains, allowing interaction with key proteins such as titin and calmodulin, which are essential for muscle function. During cardiac hypertrophy, Obscurin gene expression is upregulated, leading to additional contractile unit production, highlighting Obscurin′s importance in muscle adaptation. Studies have shown that Obscurin mRNA knockdown disrupts M-bands and A-bands organization, resulting in decreased myosin and myomesin levels, thereby underscoring Obscurin′s necessity for maintaining regular sarcomere structure. Six Obscurin isoforms are generated through alternative splicing, which may contribute to diverse functional roles in muscle physiology.

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Obscurin Antibody (5C20) References:

1. Obscurin is a ligand for small ankyrin 1 in skeletal muscle.  |  Kontrogianni-Konstantopoulos, A., et al. 2003. Mol Biol Cell. 14: 1138-48. PMID: 12631729
2. Obscurin regulates the organization of myosin into A bands.  |  Kontrogianni-Konstantopoulos, A., et al. 2004. Am J Physiol Cell Physiol. 287: C209-17. PMID: 15013951
3. De novo myofibrillogenesis in C2C12 cells: evidence for the independent assembly of M bands and Z disks.  |  Kontrogianni-Konstantopoulos, A., et al. 2006. Am J Physiol Cell Physiol. 290: C626-37. PMID: 16207790
4. Obscurin is required for the lateral alignment of striated myofibrils in zebrafish.  |  Raeker, MO., et al. 2006. Dev Dyn. 235: 2018-29. PMID: 16779859
5. Molecular interactions with obscurin are involved in the localization of muscle-specific small ankyrin1 isoforms to subcompartments of the sarcoplasmic reticulum.  |  Armani, A., et al. 2006. Exp Cell Res. 312: 3546-58. PMID: 16962094
6. Obscurin modulates the assembly and organization of sarcomeres and the sarcoplasmic reticulum.  |  Kontrogianni-Konstantopoulos, A., et al. 2006. FASEB J. 20: 2102-11. PMID: 17012262
7. Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band: implications for hereditary myopathies.  |  Fukuzawa, A., et al. 2008. J Cell Sci. 121: 1841-51. PMID: 18477606
8. Localization of ank1.5 in the sarcoplasmic reticulum precedes that of SERCA and RyR: relationship with the organization of obscurin in developing sarcomeres.  |  Giacomello, E. and Sorrentino, V. 2009. Histochem Cell Biol. 131: 371-82. PMID: 19002483
9. Obscurin variants and inherited cardiomyopathies.  |  Marston, S. 2017. Biophys Rev. 9: 239-243. PMID: 28510120
10. The potential of obscurin as a therapeutic target in muscle disorders.  |  Randazzo, D., et al. 2017. Expert Opin Ther Targets. 21: 897-910. PMID: 28756711
11. Obscurin is a semi-flexible molecule in solution.  |  Whitley, JA., et al. 2019. Protein Sci. 28: 717-726. PMID: 30666746
12. Obscurin regulates ankyrin macromolecular complex formation.  |  Subramaniam, J., et al. 2022. J Mol Cell Cardiol. 168: 44-57. PMID: 35447147