Tropomyosin β Antibody (3C8): sc-293374

Tropomyosin β Antibody (3C8) is a mouse monoclonal IgG2a kappa light chain antibody that detects Tropomyosin beta protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). Anti-Tropomyosin beta antibody (3C8) is available as the non-conjugated format. Tropomyosin β, also known as TPM2 or TMSB, is a 284 amino acid protein that plays a crucial role in muscle contraction and cytoskeletal stability by binding to actin filaments in both muscle and non-muscle cells. This binding is essential for the regulation of striated muscle contraction, as binding helps maintain the structural integrity of the cytoskeleton, which is vital for cellular shape and movement. Additionally, Tropomyosin β is expressed in various isoforms and has been implicated in the pathology of primary breast cancer, indicating a potential role in tumor formation and metastasis. Furthermore, mutations in the gene encoding Tropomyosin β are associated with serious conditions such as nemaline myopathy type 4 and distal arthrogryposis type 1, highlighting the importance of Tropomyosin β in muscle function and development.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

Tropomyosin β Antibody (3C8) References:

1. Mutations in the beta-tropomyosin (TPM2) gene--a rare cause of nemaline myopathy.  |  Donner, K., et al. 2002. Neuromuscul Disord. 12: 151-8. PMID: 11738357
2. Beta beta homodimers exist in native rabbit skeletal muscle tropomyosin and increase after denaturation-renaturation.  |  Holtzer, ME., et al. 1992. Protein Sci. 1: 335-41. PMID: 1304342
3. Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function.  |  Robinson, P., et al. 2007. FASEB J. 21: 896-905. PMID: 17194691
4. Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation.  |  Tajsharghi, H., et al. 2007. Neurology. 68: 772-5. PMID: 17339586
5. Effects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibres.  |  Ochala, J., et al. 2007. J Physiol. 581: 1283-92. PMID: 17430991
6. Congenital myopathy with nemaline rods and cap structures caused by a mutation in the beta-tropomyosin gene (TPM2).  |  Tajsharghi, H., et al. 2007. Arch Neurol. 64: 1334-8. PMID: 17846275
7. Beta-tropomyosin mutations alter tropomyosin isoform composition.  |  Nilsson, J. and Tajsharghi, H. 2008. Eur J Neurol. 15: 573-8. PMID: 18422639
8. Skeletal muscle contractile gene (TNNT3, MYH3, TPM2) mutations not found in vertical talus or clubfoot.  |  Gurnett, CA., et al. 2009. Clin Orthop Relat Res. 467: 1195-200. PMID: 19142688
9. Stability of two beta-tropomyosin isoforms: effects of mutation Arg91Gly.  |  Nevzorov, I., et al. 2008. J Muscle Res Cell Motil. 29: 173-6. PMID: 19214762
10. A Traditional Chinese Medicine, Maoto, Suppresses Hepatitis B Virus Production.  |  Rahman, MA., et al. 2020. Front Cell Infect Microbiol. 10: 581345. PMID: 33553000
11. Assignment of the human beta tropomyosin gene (TPM2) to band 9p13 by fluorescence in situ hybridisation.  |  Hunt, CC., et al. 1995. Cytogenet Cell Genet. 71: 94-5. PMID: 7606936
12. Fine mapping of five human skeletal muscle genes: alpha-tropomyosin, beta-tropomyosin, troponin-I slow-twitch, troponin-I fast-twitch, and troponin-C fast.  |  Tiso, N., et al. 1997. Biochem Biophys Res Commun. 230: 347-50. PMID: 9016781