The Tom (translocase of the mitochondrial outer membrane) complex consists of two integral membrane import receptors, Tom20 and Tom70 (translocase of outer mitochondrial membrane 70) and a GIP (general import pore) complex. TOM70/ TOMM70A has 12 coding exons and spans about 37kb. It is abundantly expressed in human tissues and is located on human chromosome 3q13.1-q13.2. It belongs to the tetratricopeptide repeat (TPR) co-chaperone family. TOM70 has a dicarboxylate TPR clamp domain that can interact with molecular chaperones like Hsp70 (heat shock protein 70)/Hsc70 and/or Hsp90.
Immunogen
TOM70 antibody was raised against a 17 amino acid peptide near the amino terminus of human TOM70.
Biochem/physiol Actions
TOM70/ TOMM70A (translocase of outer mitochondrial membrane 70) has the capability to identify preproteins with internal hydrophobic targeting sequences. It contributes in the transportation of several large hydrophobic matrix proteins. The import receptor Tom70 acts as a docking site for cytosolic multichaperone complexes.
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Linkage
The action of this antibody can be blocked using blocking peptide SBP3500459.
Physical form
Supplied in PBS with 0.02% sodium azide.
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The Journal of biological chemistry, 286(37), 32208-32219 (2011-07-21)
The mitochondrial import receptor Tom70 contains a tetratricopeptide repeat (TPR) clamp domain, which allows the receptor to interact with the molecular chaperones, Hsc70/Hsp70 and Hsp90. Preprotein recognition by Tom70, a critical step to initiate import, is dependent on these cytosolic
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