Overview
- Peptide (C)DNHGAPHGMGLGTQHS, corresponding to amino acid residues 259-274 of rat TRIC-A (Accession A6ZIQ8). Intracellular, C-terminus.
Western blot analysis of rat brain lysate (lanes 1 and 4), and mouse brain membrane (lanes 2 and 5) and skeletal muscle (lanes 3 and 6):1-3. Anti-TRIC-A (TMEM38A) Antibody (#ATC-002), (1:200).
4-6. Anti-TRIC-A (TMEM38A) Antibody, preincubated with TRIC-A/TMEM38A Blocking Peptide (#BLP-TC002).
Expression of TRIC-A in rat skeletal muscleImmunohistochemical staining of paraffin-embedded rat skeletal muscle sections using Anti-TRIC-A (TMEM38A) Antibody (#ATC-002), followed by goat anti-rabbit-AlexaFluor-594 secondary antibody. A. TRIC-A labeling (red) appears in the edges of the muscle fibers, where the endomysium is present. B. Nuclear staining using DAPI as the counterstain. C. Merged images of A and B.
Expression of TRIC-A in mouse muscle myoblast (C2C12) cell lineImmunocytochemical staining of mouse paraformaldehyde-fixed and permeabilized muscle myoblast (C2C12) cell line. A. Cells were stained with Anti-TRIC-A (TMEM38A) Antibody (#ATC-002), (1:200) followed by goat anti-rabbit-AlexaFluor-594 secondary antibody (red). B. Nuclear staining using DAPI as the counterstain (blue). C. Merged images of panels A and B.
- Weisleder, N. et al. (2008) Cell Calcium 43, 1.
- Zhao, X. et al. (2010) J. Biol. Chem. 285, 37370.
- Silverio, A.L. and Saier, M.H. Jr. (2011) J. Memb. Biol. 241, 77.
- Yazawa, M. et al. (2007) Nature 448, 78.
- Yamazaki, D. et al. (2009) Pharmacol. Ther. 121, 265.
Intracellular Ca2+ levels are important in proper cellular functions and have prominent roles in various cell signaling pathways and are crucial for muscle contractions. Indeed, an important step leading to muscle contraction is the massive release of Ca2+ ions from the endoplasmic/sarcoplasmic reticulum (ER/SR) to the cytosol. A battery of results suggest that specific K+ channels are important to counteract the Ca2+ outflow in order to neutralize the negative potential created by the movement of Ca2+ ions. It is believed that TRIC channels are responsible for neutralizing this negative potential1,2.
Trimeric intracellular cation-specific (TRIC) channels are critical for proper management of intracellular stores. TRIC-A and TRIC-B both belong to this family and are both permeable to monovalent ions with a preference for K+ 3. Both channels are localized to the ER/SR membrane. Each TRIC subunit contains three transmembrane domains, a cytoplasmic C-terminus and a luminal N-terminus. Functional entities are formed by homotrimerizarion4. The activity of TRIC-A is regulated by voltage whereas that of TRIC-B can be regulated by different mechanisms3.
Knockout studies of these channels have shown that TRIC-A knockout mice are viable while those of TRIC-B die at the neonatal stage5.
TRIC-A is mostly expressed in excitable tissues like the brain and muscle while TRIC-B is ubiquitously expressed.
Anti-TRIC-A (TMEM38A) Antibody (#ATC-002) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunohistochemistry, and immunocytochemistry applications. It has been designed to recognize TRIC-A from rat and mouse samples. The antibody is not suited to recognize TRIC-A from human samples.
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