|Application ||WB, IHC-P, FC, E|
|Calculated MW||48910 Da|
|Antigen Region||383-410 aa|
|Other Names||Protoheme IX farnesyltransferase, mitochondrial, 251-, Heme O synthase, COX10|
|Target/Specificity||This COX10 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 383-410 amino acids from the C-terminal region of human COX10.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||COX10 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Converts protoheme IX and farnesyl diphosphate to heme O.|
|Cellular Location||Mitochondrion membrane; Multi-pass membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes heme A:farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion.
Chen, Z., et al. Oncogene 29(30):4362-4368(2010)
Vitali, M., et al. J Neural Transm 116(12):1635-1641(2009)
Dassa, E.P., et al. EMBO Mol Med 1(1):30-36(2009)
Veluthakal, R., et al. Diabetes 56(1):204-210(2007)
Coenen, M.J., et al. Ann. Neurol. 56(4):560-564(2004)
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