ATP5G1 Blocking Peptide (Center)
€293.00
In stock
SKU
AC-BP22100c
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.
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
Type: Synthetic peptide
Primary Accession: P05496
Other Accession: P32876;Q9CR84;A1XQS5;Q06645;P17605;P07926;Q06055;P56383;Q5RAP9;Q06646;Q06056;Q3ZC75;P48201;P56384;Q5RFL2;Q71S46
Gene ID: 516
Gene Name: ATP5MC1 (HGNC:841)
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.
Bio 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).
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.
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
Type: Synthetic peptide
Primary Accession: P05496
Other Accession: P32876;Q9CR84;A1XQS5;Q06645;P17605;P07926;Q06055;P56383;Q5RAP9;Q06646;Q06056;Q3ZC75;P48201;P56384;Q5RFL2;Q71S46
Gene ID: 516
Gene Name: ATP5MC1 (HGNC:841)
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.
Bio 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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