Comparison

Recombinant Human ATP synthase subunit beta, mitochondrial(ATP5F1B),partial

Item no. CSB-EP002350HU1-10
Manufacturer Cusabio
Amount 10ug
Quantity options 1mg 10ug 100ug 20ug 200ug 50ug 500ug
Category
Type Proteins Recombinant
Format Liquid or Lyophilized powder
Specific against other
Conjugate/Tag Myc
Purity Greater than 85% as determined by SDS-PAGE.
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Available
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

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 10ug
Available: In stock
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