Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
Pathway
Metabolism of proteins, organism-specific biosystem; Mitochondrial Protein Import, organism-specific biosystem.
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
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Amick, J; Schlanger, SE; et al. Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone. PROTEIN SCIENCE 23:833-842(2014).
Yan, J; Takahashi, T; et al. Combined linkage analysis and exome sequencing identifies novel genes for familial goiter. JOURNAL OF HUMAN GENETICS 58:366-377(2013).
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COA
Certificate of Analysis