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ATP5G1 Blocking Peptide (Center)

Synthetic peptide

     
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Product Information
Primary Accession P05496
Other Accession P32876, Q9CR84, A1XQS5, Q06645, P17605, P07926, Q06055, P56383, Q5RAP9, Q06646, Q06056, Q3ZC75, P48201, P56384, Q5RFL2, Q71S46
Additional Information
Gene ID 516
Other Names ATP synthase F(0) complex subunit C1, mitochondrial, ATP synthase lipid-binding protein, ATP synthase proteolipid P1, ATP synthase proton-transporting mitochondrial F(0) complex subunit C1, ATPase protein 9, ATPase subunit c, ATP5G1
Target/Specificity The synthetic peptide sequence is selected from aa 61-71 of HUMAN ATP5G1
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 ATP5G1
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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Cellular Location Mitochondrion membrane; Multi-pass membrane protein
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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

References

Dyer M.R.,et al.Biochem. J. 293:51-64(1993).
Higuti T.,et al.Biochim. Biophys. Acta 1173:87-90(1993).
Wiemann S.,et al.Genome Res. 11:422-435(2001).
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Farrell L.B.,et al.Biochem. Biophys. Res. Commun. 144:1257-1264(1987).

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$ 80.00
Cat# BP22100c
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