D1-Int Antikörper
PsbA
Reaktivität: Arabidopsis, Cyanobacteria (Nostoc), Nicotiana tabacum
WB
Wirt: Kaninchen
Polyclonal
unconjugated
1 image
(2 Referenzen)-
- Target
- D1-Int (PsbA)
- Reaktivität
- Arabidopsis, Cyanobacteria (Nostoc), Nicotiana tabacum
- Wirt
- Kaninchen
- Klonalität
- Polyklonal
- Applikation
- Western Blotting (WB)
- Spezifität
- Higher plants, cyanobacteria. Antibody reacts with a 32 kDa protein in all tested photosynthetic organisms
- Immunogen
- synthetic peptide (a. a. 57 – 85) against PsbA2/3 proteins from Synechocystis sp. PCC 6803. The peptide is conservative in D1 protein sequences form all photosynthetic organisms.
- Isotyp
- IgG
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- Applikationshinweise
- Western blot (1 : 1.000 for ECL)
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Lagerung
- 4 °C
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: "The Arabidopsis thylakoid protein PAM68 is required for efficient D1 biogenesis and photosystem II assembly." in: The Plant cell, Vol. 22, Issue 10, pp. 3439-60, (2010) (PubMed).
: "Oxidative stress induces distinct physiological responses in the two Trebouxia phycobionts of the lichen Ramalina farinacea." in: Annals of botany, Vol. 107, Issue 1, pp. 109-18, (2010) (PubMed).
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: "The Arabidopsis thylakoid protein PAM68 is required for efficient D1 biogenesis and photosystem II assembly." in: The Plant cell, Vol. 22, Issue 10, pp. 3439-60, (2010) (PubMed).
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- Target
- D1-Int (PsbA)
- Hintergrund
- D1 is one the major proteins of the reaction centre of photosystem II which carries the Q B -binding site. D1 reduces the reaction centre P680* and provides the ligands to the manganese cluster of the water-oxidizing complex at the lumenal side of thylakoid membrane. D1 protein is synthesized in a precursor form containing a C-terminal extension of 16 amino acid residues in cyanobacteria and 8 – 9 - in eukaryotes. The precursor D1 is co-translationally inserted into the thylakoid membrane and is C-terminally cleaved by CtpA protease (Anbudurai et al., 1994, PNAS 16, 8082 – 8086). D1 protein from higher plants and green algae can be phosphorylated by STN8 kinase (Bonardi et al., 2005, Nature 437, 1179 – 1182, Vaionen et al., 2005, J Biol. Chem. 280, 33679 – 33686).
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