ArtNr |
CSB-EP002350HU1-200 |
Hersteller |
Cusabio
|
Menge |
200ug |
Quantity options |
1mg
10ug
100ug
20ug
200ug
50ug
500ug
|
Kategorie |
|
Typ |
Proteins Recombinant |
Format |
Liquid or Lyophilized powder |
Specific against |
other |
Konjugat/Tag |
Myc |
Purity |
Greater than 85% as determined by SDS-PAGE. |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Lieferbar |
|
Research areas |
Tags & Cell Markers |
Target / Protein |
ATP5B |
Biologically active |
Not Test |
Expression system |
E.coli |
Species of origin |
Homo sapiens (Human) |
Uniprot ID |
P06576 |
AA Sequence |
YSVFAGVGERTREGNDLYHEMIESGVINLKDATSK VALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQ DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT LATDMGTMQERITTTKKGSITSVQAIYVPADDLTD PAPATTFAHLDATTVLSRAIAELGIYPAVDPLDST SRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIA ILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVF TGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYM VGPIEEAVAKADKLAEEHSS |
Tag Info |
N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged |
Expression Region |
230-529aa |
Protein length |
Partial |
MW |
52.8 kDa |
Alternative Name(s) |
ATPMB, ATPSB |
Relevance |
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. |
References |
"The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression." Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C. Genomics 5:829-843(1989) |
Purity |
Greater than 85% as determined by SDS-PAGE. |
Storage |
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C. |
Notes |
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week. |
Function |
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. |
Subcellular Location |
Mitochondrion, Mitochondrion inner membrane |
Protein Families |
ATPase alpha/beta chains family |
Paythway |
OxidativePhosphorylation |
Tag Information |
N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged |
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