TOM70 (E7E1M) Rabbit mAb #65619

Mitochondria play a central role in cellular energy metabolism and are essential organelles in eukaryotes. In humans, 13 proteins are encoded by the mitochondrial genome, while the vast majority of mitochondrial proteins are encoded by the nuclear genome. As a result, most mitochondrial proteins are synthesized as precursors in the cytoplasm and imported across mitochondrial membranes by one or more translocase protein complexes (1). The translocase of the outer mitochondrial membrane (TOM complex) facilitates the import of proteins through the outer mitochondrial membrane, while the complementary translocase of the inner membrane (TIM complex) is responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors TOM20, TOM22, TOM70, and the channel-forming protein TOM40 (1).

TOM70 serves as a docking partner for cytosolic chaperone proteins and thus participates in the uptake of newly synthesized chaperone-bound proteins during mitochondrial biogenesis (2). In addition, TOM70 may play a role in Parkinson's disease since it is involved in recruiting PINK1 and Parkin to mitochondria. PINK1 and Parkin are activated after mitochondrial membrane depolarization, thus identifying uncoupled and damaged mitochondria (3). In addition, the protein encoded by Orf9b in the genome of SARS-CoV-2 binds to TOM70, leading to suppression of interferon responses (4).