Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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.
Development References (3)
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Moro F, Sirrenberg C, Schneider HC, Neupert W, Brunner M. The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix. EMBO J. 1999; 18(13):3667-3675. (Biology). View Reference
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Rassow J, Dekker PJ, van Wilpe S, Meijer M, Soll J. The preprotein translocase of the mitochondrial inner membrane: function and evolution. J Mol Biol. 1999; 286(1):105-120. (Biology). View Reference
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Ryan KR, Leung RS, Jensen RE. Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules. Mol Cell Biol. 1988; 18(1):178-187. (Biology). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
