protein

Recombinant Mouse ATP synthase subunit beta, mitochondrial

MBS953423

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Mouse ATP synthase subunit beta, mitochondrial

ATP synthase subunit beta

ATP synthase subunit beta, mitochondrial; ATP synthase subunit beta, mitochondrial; ATP synthase subunit beta, mitochondrial; ATP synthase, H+ transporting mitochondrial F1 complex, beta subunit

Atp5b

Atp5b; Atp5b

ATPB_MOUSE

E Coli or Yeast or Baculovirus or Mammalian Cell

47-529

529

AAQASAAPKAGTATGRIVAVIGAVVDVQFDEGLPPILNA
LEVQGRDSRLVLEVAQHLGESTVRTIAMDGTEGLVRGQK
VLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQF
APIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKI
GLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTR
EGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARA
RVALTGLTVAEYFRDQEGQDV

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

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 alpha and beta 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 beta subunits.

A novel principle for conferring selectivity to poly(A) -binding proteins interdependence of two ATP synthase beta-subunit mRNA-binding proteins.Andersson U., Antonicka H., Houstek J., Cannon B.Biochem. J. 346:33-39(2000) Housekeeping genes for phylogenetic analysis of eutherian relationships.Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.Mol. Biol. Evol. 23:1493-1503(2006) Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.Submitted (JUL-2007) to UniProtKB Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS.Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.Mol. Cell. Proteomics 6:669-676(2007) Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels.Chinopoulos C., Konrad C., Kiss G., Metelkin E., Torocsik B., Zhang S.F., Starkov A.A.FEBS J. 278:1112-1125(2011) SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.Mol. Cell 50:919-930(2013) Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013)

31980648

NP_058054.2

NM_016774.3

P56480

67.7kD

Alzheimer's Disease Pathway (83294); Alzheimer's Disease Pathway (509); Electron Transport Chain Pathway (198400); F-type ATPase, Eukaryotes Pathway (522571); F-type ATPase, Eukaryotes Pathway (890450); Formation Of ATP By Chemiosmotic Coupling Pathway (1324386); Huntington's Disease Pathway (83297); Huntington's Disease Pathway (512); Metabolic Pathways (132962); Metabolism Pathway (1324226)

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: EC 3.6.3.14; Energy Metabolism - oxidative phosphorylation; Hydrolase; Mitochondrial. Cellular 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 binding. Biological 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

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750