|Other Names||Cytochrome c oxidase subunit 5A, mitochondrial, Cytochrome c oxidase polypeptide Va, COX5A|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13154a was selected from the N-term region of COX5A. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.|
|Cellular Location||Mitochondrion inner membrane.|
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Provided below are standard protocols that you may find useful for product applications.
Cytochrome c oxidase (COX) is the terminal enzyme of themitochondrial respiratory chain. It is a multi-subunit enzymecomplex that couples the transfer of electrons from cytochrome c tomolecular oxygen and contributes to a proton electrochemicalgradient across the inner mitochondrial membrane. The complexconsists of 13 mitochondrial- and nuclear-encoded subunits. Themitochondrially-encoded subunits perform the electron transfer ofproton pumping activities. The functions of the nuclear-encodedsubunits are unknown but they may play a role in the regulation andassembly of the complex. This gene encodes the nuclear-encodedsubunit Va of the human mitochondrial respiratory chain enzyme. Apseudogene COX5AP1 has been found in chromosome 14q22. [provided byRefSeq].
Chen, Z.X., et al. Cell Death Differ. 17(3):408-420(2010)Fornuskova, D., et al. Biochem. J. 428(3):363-374(2010)Uddin, M., et al. BMC Evol. Biol. 8, 8 (2008) :Williams, S.L., et al. J. Biol. Chem. 279(9):7462-7469(2004)Hofmann, S., et al. Cytogenet. Cell Genet. 83 (3-4), 226-227 (1998) :
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