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ATP5D Blocking Peptide (C-term)

Synthetic peptide

     
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Product Information
Primary Accession P30049
Other Accession P35434, Q9D3D9, P05630
Additional Information
Gene ID 513
Other Names ATP synthase subunit delta, mitochondrial, F-ATPase delta subunit, ATP5D
Target/Specificity The synthetic peptide sequence is selected from aa 156-168 of HUMAN ATP5D
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATP5F1D (HGNC:837)
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 (PubMed:29478781). 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 (PubMed:1531933).
Cellular Location Mitochondrion. Mitochondrion inner membrane.
Research Areas
Citations (0)
citation

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Background

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.

References

Jordan E.M.,et al.Biochim. Biophys. Acta 1130:123-126(1992).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Grimwood J.,et al.Nature 428:529-535(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Hochstrasser D.F.,et al.Electrophoresis 13:992-1001(1992).

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$ 277.78
Cat# BP20890c
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