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ATP5G1 Blocking Peptide (Center)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P05496 |
|---|---|
| Other Accession | P32876, Q9CR84, A1XQS5, Q06645, P17605, P07926, Q06055, P56383, Q5RAP9, Q06646, Q06056, Q3ZC75, P48201, P56384, Q5RFL2, Q71S46 |
| 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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ATP5MC1 (HGNC:841) |
|---|---|
| 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 |
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Provided below are standard protocols that you may find useful for product applications.
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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