1. Since applications vary, each investigator should titrate the reagent to obtain optimal results. 2. Please refer to us for technical protocols. 3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing. 4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Storage Comment
Store undiluted at -20° C.
Moro, Sirrenberg, Schneider, Neupert, Brunner: "The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix." in: The EMBO journal, Vol. 18, Issue 13, pp. 3667-75, (1999) (PubMed).
Rassow, Dekker, van Wilpe, Meijer, Soll: "The preprotein translocase of the mitochondrial inner membrane: function and evolution." in: Journal of molecular biology, Vol. 286, Issue 1, pp. 105-20, (1999) (PubMed).
Ryan, Leung, Jensen: "Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules." in: Molecular and cellular biology, Vol. 18, Issue 1, pp. 178-87, (1998) (PubMed).
Target
TIMM23
(Translocase of Inner Mitochondrial Membrane 23 Homolog (Yeast) (TIMM23))
Mitochondria, the site of cellular energy production, must import all proteins necessary for their function. Import is mediated by two mechanisms: the translocase of the outer membrane (Tom) and the translocase of the inner membrane (Tim). Tim23 and Tim17 are integral membrane proteins that associate to form the import channel for mitochondrial preproteins that contain N-terminal hydrophilic sequences. They also associate with Tim44, an adaptor for the membrane binding of mtHsp70, a matrix heat shock protein, which drives the import of the processed preprotein. The N-terminal intermembrane space domain of Tim23 contains a leucine zipper motif and mediates the formation of a Tim23 dimer. As an imported protein passes through the TOM machinery, its N-terminal matrix targeting sequence interacts with the Tim23 dimer. This induces the dissociation of the dimer and initiation of inner membrane translocation of the presequence. In addition to its 9 kDa N-terminal hydrophilic segment, Tim23 contains a 14 kDa hydrophobic domain with four predicted membrane spans. Thus, Tim23 is an important integral membrane component of the mitochondrial protein translocation machinery.