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ATP5F1 Blocking Peptide (Center)

Synthetic peptide

     
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Product Information
Primary Accession P24539
Additional Information
Gene ID 515
Other Names ATP synthase F(0) complex subunit B1, mitochondrial, ATP synthase proton-transporting mitochondrial F(0) complex subunit B1, ATP synthase subunit b, ATPase subunit b, ATP5F1
Target/Specificity The synthetic peptide sequence is selected from aa 181-195 of Human ATP5F1
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
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 ATP5F1
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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Cellular Location Mitochondrion. Mitochondrion inner membrane.
Research Areas
Citations (0)

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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 synthesis 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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.

References

Higuti T., et al. Biochem. Biophys. Res. Commun. 178:1014-1020(1991).
Gregory S.G., et al. Nature 441:315-321(2006).
Choudhary C., et al. Science 325:834-840(2009).
Burkard T.R., et al. BMC Syst. Biol. 5:17-17(2011).

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$ 80.00
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Cat# BP20527c
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