The ATP5F1B Polyclonal Antibody (PAC025144) is a valuable tool for researchers studying ATP5F1B, a key subunit of the mitochondrial membrane ATP synthase complex involved in cellular energy production. This antibody, generated in rabbits, exhibits high specificity and sensitivity when used with human samples, making it suitable for Western blot analysis.ATP5F1B is essential for the synthesis of ATP, the primary energy currency of the cell, and its dysfunction has been linked to various metabolic disorders and diseases. By targeting ATP5F1B, researchers can gain insights into mitochondrial function and dysfunction, paving the way for potential therapeutic interventions in conditions such as neurodegenerative diseases, metabolic disorders, and cancer.
The ATP5F1B Polyclonal Antibody is a reliable tool for exploring the biological role of ATP5F1B and its implications in various physiological and pathological processes. Its specificity, sensitivity, and versatility make it an indispensable asset for studies focusing on mitochondrial biology, energy metabolism, and related disease mechanisms.
Antibody Name:
Atp5f1b Antibody (PACO25144)
Antibody SKU:
PACO25144
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Mouse
Immunogen:
Recombinant Mouse ATP synthase subunit beta, mitochondrial protein (47-529AA)
Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits α and β form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the β subunits.
Synonyms:
ATP synthase subunit beta, mitochondrial (ATP synthase F1 subunit beta), Atp5f1b, Atp5b
UniProt Protein Function:
ATP5B: 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. Belongs to the ATPase alpha/beta chains family.Protein type: Energy Metabolism - oxidative phosphorylation; EC 3.6.3.14; Mitochondrial; HydrolaseCellular Component: cell surface; membrane; mitochondrial inner membrane; mitochondrial membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrion; myelin sheath; nucleus; plasma membrane; proton-transporting ATP synthase complex, catalytic core F(1)Molecular Function: ATP binding; ATPase activity; calcium ion binding; hydrogen ion transporting ATP synthase activity, rotational mechanism; hydrogen ion transporting ATPase activity, rotational mechanism; hydrolase activity; hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; lipoprotein receptor activity; MHC class I protein binding; nucleotide bindingBiological Process: angiogenesis; ATP biosynthetic process; ATP hydrolysis coupled proton transport; ATP metabolic process; ATP synthesis coupled proton transport; ion transport; lipid metabolic process; osteoblast differentiation; proton transport; receptor-mediated endocytosis; regulation of intracellular pH; substrate-bound cell migration, cell release from substrate; transport