Recombinant Human ATP synthase subunit delta, mitochondrial (ATP5D), partial

Product Description

Recombinant Human ATP synthase subunit delta, mitochondrial (ATP5D), partial is available at Gentaur for Next week Delivery.

Gene Name: ATP5D

Alternative Names : F-ATPase delta subunit

Expression Region : 43-161aa

AA Sequence : ASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANE

Sequence Info : Partial

Tag Info : N-terminal GST-tagged

Theoretical MW : 39.4 kDa

Storage Buffer : 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.

Endotoxin Level : Not tested-

Biological Activity : Not tested

Storage : Short term: -20°C; Long term: -80°C. Minimize freeze and thaw cycles.

Research Area : Metabolism

Restriction : For Research Use Only. Not for use in diagnostic procedures, drug use, or for administration to humans or animals.

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.

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.

Involvement in disease :

Subcellular location : Mitochondrion, Mitochondrion inner membrane

Protein Families : ATPase epsilon chain family

Tissue Specificity :

Paythway : OxidativePhosphorylation

Uniprot ID : P30049