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Western blot analysis of extracts from HL60 cells lyastes.using COX6B1 Rabbit mAb [PGR3] at dilution of 1:1000 incubated at 4℃ over night
Protein names :COX6B1,COX6B,CX6B1_HUMAN,Cytochrome c oxidase subunit 6B1
UniProtID :P14854
MASS(da) :10,192
MW(kDa) :10 kDa
Form :Liquid
Purification :Protein A purification
Host :Rabbit
Isotype :IgG
sensitivity :Endogenous
Reactivity :Human
Specificity :Antibody is produced by immunizing animals with a synthetic peptide of Human COX6B1.
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 :HL60 cells lyastes
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,Peripheral membrane protein,Intermembrane side.
IMPORTANT: For western blots, incubate membrane with diluted primary antibody in 1% w/v BSA, 1X TBST at 4°C overnight.