protein

Recombinant Human ATP synthase subunit beta, mitochondrial (ATP5B)

MBS964125

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human ATP synthase subunit beta, mitochondrial (ATP5B)

ATP synthase subunit beta, mitochondrial (ATP5B)

ATP synthase subunit beta, mitochondrial; EC=3.6.3.14

ATP synthase subunit beta, mitochondrial; ATP synthase subunit beta, mitochondrial; ATP synthase subunit beta, mitochondrial; epididymis secretory protein Li 271; mitochondrial ATP synthase beta subunit; mitochondrial ATP synthetase, beta subunit; ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide

ATP5B

ATP5B; ATPMB; ATPSB

ATP5B; ATP5B; ATPMB; ATPSB; HEL-S-271; ATPMB; ATPSB

ATPB_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

48-529, Mature full length protein.

529

AQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNAL
EVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKV
LDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFA
PIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIG
LFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTRE
GNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARAR
VALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSA
LLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQA
IYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAV
DPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDI
IAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTG
HMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEE
AVAKADKLAEEHSS

>90%

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Species: Homo sapiens (Human)

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.

32189394

NP_001677.2

NM_001686.3

P06576

68kD

Alzheimer's Disease Pathway (83097); Alzheimer's Disease Pathway (509); Electron Transport Chain Pathway (198860); F-type ATPase, Eukaryotes Pathway (522535); Formation Of ATP By Chemiosmotic Coupling Pathway (105922); Huntington's Disease Pathway (83100); Huntington's Disease Pathway (512); Metabolism Pathway (477135); Metabolism Of Proteins Pathway (106230); Mitochondrial Protein Import Pathway (576261)

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core. [provided by RefSeq, Jul 2008]

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; Hydrolase; Mitochondrial. Chromosomal Location of Human Ortholog: 12q13.13. Cellular Component: mitochondrial proton-transporting ATP synthase, catalytic core; cell surface; membrane; mitochondrion; mitochondrial matrix; mitochondrial membrane; plasma membrane; nucleus; mitochondrial proton-transporting ATP synthase complex. Molecular Function: protein binding; MHC class I protein binding; transporter activity; ATPase activity; hydrogen ion transporting ATP synthase activity, rotational mechanism; transmembrane transporter activity; hydrogen ion transporting ATPase activity, rotational mechanism; ATP binding. Biological Process: mitochondrion organization and biogenesis; substrate-bound cell migration, cell release from substrate; generation of precursor metabolites and energy; organelle organization and biogenesis; osteoblast differentiation; cellular metabolic process; proton transport; ATP biosynthetic process; regulation of intracellular pH; ATP hydrolysis coupled proton transport; mitochondrial ATP synthesis coupled proton transport; lipid metabolic process; angiogenesis

0.05 mg (E-Coli)

180 USD

0.05 mg (Yeast)

260

0.2 mg (E-Coli)

490

0.2 mg (Yeast)

600

0.5 mg (E-Coli)

715