protein

COX5B Protein, Human (His)

HY-P75686

5 μg;10 μg;50 μg

50;75;190 USD

COX5B Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

50;75;190 USD

The COX5B protein is a component of cytochrome c oxidase, the final enzyme in the mitochondrial electron transport chain. COX5B Protein, Human (His) is the recombinant human-derived COX5B protein, expressed by E. coli , with N-His labeled tag. The total length of COX5B Protein, Human (His) is 98 a.a., with molecular weight of ~14 kDa.

Human

COX5B, an integral component of the cytochrome c oxidase, stands as the final enzyme in the mitochondrial electron transport chain, orchestrating oxidative phosphorylation. This respiratory chain encompasses three crucial 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)—cooperatively facilitating the transfer of electrons derived from NADH and succinate to molecular oxygen. This intricate process generates an electrochemical gradient across the inner membrane, propelling transmembrane transport and driving ATP synthase. Cytochrome c oxidase serves as the linchpin of the respiratory chain, catalyzing the reduction of oxygen to water. Electrons, originating from reduced cytochrome c in the intermembrane space, traverse through intermediates like the dinuclear copper A center (CU(A)) in subunit 2 and heme A in subunit 1. Ultimately, this electron transfer converges at the active site in subunit 1, forming a binuclear center (BNC) composed of heme A3 and copper B (CU(B)). The BNC efficiently reduces molecular oxygen to two water molecules, utilizing four electrons from cytochrome c in the intermembrane space and four protons from the mitochondrial matrix. COX5B plays a pivotal role in energy metabolism, contributing significantly to the intricate processes of oxidative phosphorylation.

Cytochrome c oxidase subunit 5B, mitochondrial; COX5B

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4, 10% Glycerin.

Room temperature in continental US; may vary elsewhere.