Item no. |
CSB-YP002350HU-20 |
Manufacturer |
Cusabio
|
Amount |
20ug |
Category |
|
Type |
Proteins Recombinant |
Format |
Liquid or Lyophilized powder |
Specific against |
Human |
Host |
Yeast |
Purity |
Greater than 90% as determined by SDS-PAGE. |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Available |
|
Research Areas |
Tags & Cell Markers |
Target / Protein |
ATP5F1B |
Biologically Active |
Not Test |
Expression System |
Yeast |
Species of origin |
Homo sapiens (Human) |
Uniprot ID |
P06576 |
AA Sequence |
AQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPI LNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTE GLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPI DERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGI KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN VAKAHGGYSVFAGVGERTREGNDLYHEMIESGVIN LKDATSKVALVYGQMNEPPGARARVALTGLTVAEY FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPS AVGYQPTLATDMGTMQERITTTKKGSITSVQAIYV PADDLTDPAPATTFAHLDATTVLSRAIAELGIYPA VDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYK SLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQP FQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHL PEQAFYMVGPIEEAVAKADKLAEEHSS |
Tag Info |
N-terminal 6xHis-tagged |
Expression Region |
48-529aa |
Protein Length |
Full length of mature protein |
MW |
53.8 kDa |
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. |
Reference |
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 90% as determined by SDS-PAGE. |
Form |
Liquid or Lyophilized powder |
Buffer |
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20C/-80C. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
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 6xHis-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.