Triadin Antibody (IIG12): sc-59724

Triadin Antibody (IIG12) is a mouse monoclonal IgG1 kappa light chain antibody that detects Triadin protein of mouse, rat, and rabbit origin by western blotting (WB) and immunoprecipitation (IP). Anti-Triadin antibody (IIG12) is available as a non-conjugated format. Triadin is a crucial junctional terminal cisternae protein predominantly found in human skeletal muscle, encoded by the TRDN gene located on chromosome 6q22.31. Triadin plays a vital role in calcium signaling by anchoring calsequestrin to the sarcoplasmic reticulum, which is essential for proper functioning of the ryanodine receptor (RyR). Triadin′s interaction with RyR regulates calcium release during muscle contraction, influencing muscle excitability and contraction strength. Triadin inhibits calcium channel activity of RyR in skeletal muscle, ensuring tight control of calcium levels during muscle activity. Triadin′s co-localization with RyR in the junctional sarcoplasmic reticulum membrane highlights its importance in maintaining structural and functional integrity of calcium release units in muscle cells.

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Triadin Antibody (IIG12) References:

1. Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor.  |  Groh, S., et al. 1999. J Biol Chem. 274: 12278-83. PMID: 10212196
2. Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium.  |  Kobayashi, YM. and Jones, LR. 1999. J Biol Chem. 274: 28660-8. PMID: 10497235
3. Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers.  |  Sacchetto, R., et al. 1999. J Muscle Res Cell Motil. 20: 403-15. PMID: 10531621
4. Triadin: a multi-protein family for which purpose?  |  Marty, I. 2004. Cell Mol Life Sci. 61: 1850-3. PMID: 15289928
5. Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95,000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesicles.  |  Caswell, AH., et al. 1991. Biochemistry. 30: 7507-13. PMID: 1649631
6. Binding sites of monoclonal antibodies and dihydropyridine receptor alpha 1 subunit cytoplasmic II-III loop on skeletal muscle triadin fusion peptides.  |  Fan, H., et al. 1995. Biochemistry. 34: 14893-901. PMID: 7578101
7. Detection and localization of triadin in rat ventricular muscle.  |  Brandt, NR., et al. 1993. J Membr Biol. 131: 219-28. PMID: 7684084
8. Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin).  |  Knudson, CM., et al. 1993. J Biol Chem. 268: 12646-54. PMID: 7685347
9. Triad formation: organization and function of the sarcoplasmic reticulum calcium release channel and triadin in normal and dysgenic muscle in vitro.  |  Flucher, BE., et al. 1993. J Cell Biol. 123: 1161-74. PMID: 8245124
10. Biochemical characterization of ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin).  |  Knudson, CM., et al. 1993. J Biol Chem. 268: 12637-45. PMID: 8389762
11. Dual regulation of the skeletal muscle ryanodine receptor by triadin and calsequestrin.  |  Ohkura, M., et al. 1998. Biochemistry. 37: 12987-93. PMID: 9737879