Anti-TIMM8A/DDP Antibody Picoband® Fluoro594 Conjugated

Mitochondrial import inner membrane translocase subunit Tim8 A, also known as Deafness-dystonia peptide or protein is an enzyme that in humans is encoded by the TIMM8A gene. This translocase is involved in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial inner membrane. The gene is mutated in Mohr-Tranebjaerg syndrome/Deafness Dystonia Syndrome (MTS/DDS) and it is postulated that MTS/DDS is a mitochondrial disease caused by a defective mitochondrial protein import system. Defects in this gene also cause Jensen syndrome; an X-linked disease with opticoacoustic nerve atrophy and muscle weakness. This protein, along with TIMM13, forms a 70 kDa heterohexamer. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

Cadherins, Calcium Binding Proteins, Calcium Signaling, Cancer, Cell Adhesion, Cytoskeleton/ECM, Invasion/Microenvironment, Plasma Membrane, Signal Transduction, Signaling Pathway, Subcellular Markers, Tags & Cell Markers

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May play an important role in retinal development.

1. Aguirre, L. A., del Castillo, I., Macaya, A., Meda, C., Villamar, M., Moreno-Pelayo, M. A., Moreno, F. A novel mutation in the gene encoding TIMM8a, a component of the mitochondrial protein translocase complexes, in a Spanish familial case of deafness-dystonia (Mohr-Tranebjaerg) syndrome. Am. J. Med. Genet. 140A: 392-397, 2006. 2. Ezquerra, M., Campdelacreu, J., Munoz, E., Tolosa, E., Marti, M. J. A novel intronic mutation in the DDP1 gene in a family with X-linked dystonia-deafness syndrome. Arch. Neurol. 62: 306-308, 2005. 3. Hofmann, S., Rothbauer, U., Muhlenbein, N., Neupert, W., Gerbitz, K.-D., Brunner, M., Bauer, M. F. The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1-TIM13 complexes in the mitochondrial intermembrane space. J. Biol. Chem. 277: 23287-23293, 2002.