Lhcb2 | LHCII type II chlorophyll a/b-binding protein
AS01 003 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Photosynthetic eukaryotes including A. thaliana, A. hypogaea, C. quitensis Kunt Bartl, C. sativa, H. vulgare, Ch. reinhardtii, L. esculentum (Solanum lycopersicon), M. crystallinum, N. tabacum, O. sativa, P. patens, P. sativum, P. vulgaris, S. alba, S. oleracea, T. aestivum, Triticale, Z. mays
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BSA-conjugated synthetic peptide derived from a highly conserved sequence of Lhcb2 proteins from angiosperms (monocots and dicots) and gymnosperms, including Arabidopsis thaliana Lhcb2.1 UniProt: Q9SHR7, TAIR: AT2G05100, Lhcb2.2 UniProt: Q9S7J7, TAIR:AT2G05070, Lhcb2.3 UniProt:Q9XF87, TAIR:AT3G27690
28.6 | 25 kDa for Arabidopsis thaliana
Total proteins from Arabidopsis thaliana (1), (3), Chlamydomonas reinhardtii (2),(4) and Acer pseudoplatanus (5) were extracted with 2% SDS in 100mM TRIS-HCl, pH 6.8, with protease inhibitor denatured with 100 mM DTT at 85°C for 5 min were separated on 12% SDS-PAGE and blotted for 1h to nitrocellulose membrane using semi-dry transfer. Blots were blocked with 5% milk overnight at 4°C with agitation. Blot was incubated in the primary antibody at a dilution of 1:2000 for 1h at RT with agitation in TBS-T. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:25 000 for 1h at RT with agitation. The blot was washed as above and developed with chemiluminescent detection reagent. Exposure time was 10 seconds.
Courtesy Dr, Thomas Roach, University of Innsbruck, Austria
Antibody format is a total IgG fraction, which means that it is a pool of polyclonal antibodies obtained by purification of serum on Protein G, not on a specific antigen (peptide) column.
Immunoprecipitation has been done using Immunoprecipitation kit from Roche, Cat.No. 11 719 386 001.
Protein is processed into mature form (Jansson 1999).
The major light-harvesting antenna complex II (LHCII) in photosynthetic 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. Lhcb2 is often coded by several nuclear genes and is found together with Lhcb1 within the mobile LHCII trimers involved in state1-state2 transition.
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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Cantrell and Peers (2017). A mutant of Chlamydomonas without LHCSR maintains high rates of photosynthesis, but has reduced cell division rates in sinusoidal light conditions. PLoS One. 2017 Jun 23;12(6):e0179395. doi: 10.1371/journal.pone.0179395.
Tyuereva et al. (2017). The absence of chlorophyll b affects lateral mobility of photosynthetic complexes and lipids in grana membranes of Arabidopsis and barley chlorina mutants. Photosynth Res. 2017 Apr 5. doi: 10.1007/s11120-017-0376-9. (Hordeum vulgare, western blot)
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