ATP5A1 Recombinant antilichaam [5G11] (OACA12314)

ATP synthase F1 subunit alpha

ATP synthase alpha chain, mitochondrial; ATP synthase F1 subunit alpha; ATP synthase subunit alpha, mitochondrial; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle; ATP sythase (F1-ATPase) alpha subunit; ATP5A; ATP5A1; ATP5AL2; ATPM; COXPD22; epididymis secretory sperm binding protein Li 123m; hATP1; HEL-S-123m; MC5DN4; mitochondrial ATP synthetase, oligomycin-resistant; MOM2; OMR; ORM.

498

Human|Mouse

A synthesized peptide derived from human ATP5A1

Unconjugated

Recombinant Monoclonal Antibody

Affinity Purified

Reconstitution & Storage Instructions Western Blotting/Immunoblotting (WB/IB) Protocol Immunohistochemistry (IHC) Protocol Immunocytochemistry (ICC) Protocol Enzyme-Linked ImmunoSorbent Assay (ELISA) Protocol Blocking Peptide Competition Protocol (BPCP) Immunoprecipitation (IP) Protocol Antibody Array (AA) Protocol Reconstitution & Storage Instructions Reconstitution & Storage Instructions Western Blotting/Immunoblotting (WB/IB) Protocol Western Blotting/Immunoblotting (WB/IB) Protocol Immunohistochemistry (IHC) Protocol Immunohistochemistry (IHC) Protocol Immunocytochemistry (ICC) Protocol Immunocytochemistry (ICC) Protocol Enzyme-Linked ImmunoSorbent Assay (ELISA) Protocol Enzyme-Linked ImmunoSorbent Assay (ELISA) Protocol Blocking Peptide Competition Protocol (BPCP) Blocking Peptide Competition Protocol (BPCP) Immunoprecipitation (IP) Protocol Immunoprecipitation (IP) Protocol Antibody Array (AA) Protocol Antibody Array (AA) Protocol

Mitochondrial membrane ATP synthase (F (1) F (0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F (1) - containing the extramembraneous catalytic core, and F (0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F (1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F (1) . Rotation of the central stalk against the surrounding alpha (3) beta (3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity) .

Liquid

-20°C or -80°C

ATP5F1A

ATP synthase subunit alpha, mitochondrial

ATP5F1A