Recombinant Human COX2 Protein, >90% (SDS-PAGE), high purity

Item Number

rp176701

• Product Name: Recombinant Human COX2 Protein, >90% (SDS-PAGE), high purity
• Grade: Azide Free, Carrier Free
• Specifications & Purity: Carrier Free, Azide Free, ≥90%(SDS-PAGE)
• Purity: >90% (SDS-PAGE)
• Endotoxin Concentration: ＜1.0 EU/μg
• Expression System: E. coli
• Amino Acids: 90-227aa
• Sequence: MHHHHHHVNDPSLTIKSIGHQWYWTYEYTDYGGLIFNSYMLPPLFLEPGDLRLLDVDNRVVLPIEAPIRMMITSQDVLHSWAVPTLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL
• Protein Tag: N-His
• Predicted molecular weight: 16.5 kDa
• SDS-PAGE: 13.2 kDa, under reducing conditions

Product Description

Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.
Description：
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.