Lhcb3 | LHCII type III chlorophyll a/b-binding protein
AS01 002 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Photosynthetic eukaryotes including A. thaliana, A. hypogaea, Ch. vulgaris, H. vulgare, L. esculentum (Solanum lycopersicon), M. crystallinum, N. tabacum, O. sativa, P. sativum, Prasinoderma sp., Pyramimonas sp., P. vulgaris, S. oleracea, T. aestivum, Triticale, Z. mays
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BSA-conjugated synthetic peptide derived from a highly conserved sequence of Lhcb3 proteins from angiosperms (monocots and dicots) and gymnosperms, including Arabidopsis thaliana Lhcb3 UniProt: Q9S7M0,TAIR:AT5G54270. This sequence is highly conserved even in Ginko biloba and one of the major LHCII-forms of Physcomitrella patens.
28.7 | 26 kDa for Arabidopsis thaliana
Cucumis melo, Dicots, Gymnosperms, Mosses
The major light-harvesting antenna complex II (LHCII) in photsynthetic eukaryotes is located in the thylakoid membrane of the chloroplast. It is a heterotrimeric complex formed by up to 3 different individual subtypes of chlorophyll a/b-binding proteins: Lhcb1, Lhcb2, and Lhcb3. While Lhcb1 and Lhcb2 are quite similar and regularily present in multiple gene-copies, the Lhcb3 protein differs in pigment-composition and molecular size and often is coded by only a single gene. Lhcb3 seems not to be present in the mobile LHCII trimers involved in state 1-state 2 transitions.
A molecular characterisation of the LHCII proteins can be found in Caffarri et al. (2004) A Look within LHCII: Differential Analysis of the Lhcb1−3 Complexes Building the Major Trimeric Antenna Complex of Higher-Plant Photosynthesis. Biochemistry 43 (29): 9467–9476.
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