ATP synthase subunit gamma Heavy 25nmol SEQUENCE

£260.00
  • Description

  • Application Data

Description

ATP synthase subunit gamma Heavy is derived from the ATP Synthase enzymatic complex which uses the proton-motive force produced by the electron transfer chain to synthesise ATP from ADP and inorganic phosphate. The Proline residue at position 7 has been isotopically labelled with carbon-13 (5) and nitrogen-15 (1).

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Application Data

Catalogue number crb1300717c
Molecular Weight 1234
Sequence (one letter code) SEQUENCE
Sequence (three letter code)

three letter

Purity >95%
Storage -20°C
References

Song et al (2014) ATP Synthase β-Chain Overexpression in SR-BI Knockout Mice Increases HDL Uptake and Reduces Plasma HDL Level. Int. J. Endocrinol. 2014: 356432. PMID: 25114680

Fruttero et al (2019) The Fat Body of the Hematophagous Insect, Panstrongylus megistus (Hemiptera: Reduviidae): Histological Features and Participation of the β-Chain of ATP Synthase in the Lipophorin-Mediated Lipid Transfer. J Insect Sci. 19(4) 16 PMID: 31346627

Lapaille et al. (2010) Loss of mitochondrial ATP synthase subunit beta (Atp2) alters mitochondrial and chloroplastic function and morphology in Chlamydomonas. Biochim Biophys Acta. 1797(8):1533–1539 doi:10.1016/j.bbabio.2010.04.013

Manufactured in: United Kingdom
Material Safety Data Sheet (MSDS)

ATP synthase subunit gamma Heavy is derived from the ATP Synthase (the adenosine triphosphate synthase enzymatic complex) which uses the proton-motive force produced by the electron transfer chain to synthesise ATP from ADP and inorganic phosphate. It functions in the inner mitochondrial membrane, prokaryotic members and chloroplasts.

Structurally bacterial ATP synthase contains two multisubunit domains called F1 and F0. F1 which is responsible for the catalytic activity of the ATP synthase is made up of the 5 subunits α3β3γδε and F0 contains a membrane bound sector which creates a proton channel. F1 and F0 are connected by a peripheral stalk and a central stalk which links proton translocation and catalysis. Eukaryotic ATP synthase is similar to that of bacteria in terms of topology, structure and subunit composition.

The Proline residue at position 7 has been isotopically labelled with carbon-13 (5) and nitrogen-15 (1), giving this peptide a mass increase of 6 compared to the unlabelled peptide.

ATP synthase subunit gamma Heavy 25nmol

25nmol
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