Comparison

Recombinant Human ATP synthase subunit delta, mitochondrial(ATP5D)

Item no. CSB-EP002355HU-10
Manufacturer Cusabio
Amount 10 ug
Quantity options 1 mg 10 ug 100 ug 20 ug 200 ug 50 ug 500 ug
Category
Type Proteins Recombinant
Format Liquid or Lyophilized powder
Specific against other
Host E.coli
Conjugate/Tag SUMO, HIS
Purity Greater than 90% as determined by SDS-PAGE.
Sequence AEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQ VDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDG TTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDL GAAKANLEKAQAELVGTADEATRAEIQIRIEANEA LVKALE
Protein Family ATPase epsilon chain family
Citations Molecular cloning of an import precursor of the delta-subunit of the human mitochondrial ATP synthase complex.Jordan E.M., Breen G.A.M.Biochim. Biophys. Acta 1130:123-126(1992)
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias F-ATPase delta subunit
Available
Manufacturer - Targets
ATP5D
Manufacturer - Conjugate / Tag
N-terminal 6xHis-SUMO-tagged
Storage Conditions
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.
Molecular Weight
31 kDa
General Research Areas
Metabolism
Relevance
Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core, and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary elent. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Expression Region
23-168aa
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 turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. 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
Paythway
OxidativePhosphorylation
Biologically active
Not Test
Protein length
Full Length of Mature Protein

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: 10 ug
Available: In stock
available

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