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SKU: E-AB-13841_120μL-ES
COX10 Polyclonal Antibody, 120 μL
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.
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Product Specification
Basic Information
Brands:Elabscience
Model Number:
Place of Origin:China
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Shipping:The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended.
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Concentration:0.4 mg/mL
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Shelf Life:12 months
Storage:Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
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Dilution:IHC 1:50-1:200
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Application:IHC
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Research Areas:Cancer;Metabolism;Signal Transduction
Species Reactivity:Human
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Target Synonym:2410004F01Rik;AU042636;COX10;COX10;Cytochrome c oxidase assembly protein;Cytochrome c oxidase subunit X;Heme A farnesyltransferase;Heme O synthase;OTTMUSP00000006085;Protoheme IX farnesyltransferase;mitochondrial;Protoheme IX farnesyltransferase;mitochondrial precursor;RP23-78H18.1
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Buffer:PBS with 0.05% sodium azide and 50% glycerol, PH7.4
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Clonality:Polyclonal
Conjugation:Unconjugated
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