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Western blot(SDS PAGE) analysis of extracts from HeLa cells.Using MTCO1Rabbit mAb [2PS0] at dilution of 1:1000 incubated at 4℃ over night.
Protein names :MT-CO1,COI,COXI,MTCO1,COX1_HUMAN,Cytochrome c oxidase subunit 1
UniProtID :P00395
MASS(da) :57,041
MW(kDa) :37 kDa
Form :Liquid
Purification :Protein A purification
Host :Rabbit
Isotype :IgG
sensitivity :Endogenous
Reactivity :Human,Mouse,Rat
Specificity :Antibody is produced by immunizing animals with a synthetic peptide at the sequence of human MTCO1
Storage :Antibody store in 10 mM PBS, 0.5mg/ml BSA, 50% glycerol. Shipped at 4°C. Store at-20°C or -80°C. Products are valid for one natural year of receipt.Avoid repeated freeze / thaw cycles.
WB Positive detected :HeLa cells
Function : Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix..
Subcellular locationi :Mitochondrion inner membrane,Multi-pass membrane protein.
IMPORTANT: For western blots, incubate membrane with diluted primary antibody in 1% w/v BSA, 1X TBST at 4°C overnight.