Lhcb1 | LHCII type I chlorophyll a/b-binding protein
AS01 004 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Photosynthetic eukaryotes including A. thaliana, A. hypogaea, B. napus, C. reticulata, C. vulgaris, C. quitensis Kunt Bartl, C. pumilum, H. vulgare, L. esculentum (Solanum lycopersicon), M. crystallinum, N. tabacum, O. sativa, P. sativum, P. vulgaris, R. discolor, S. alaba, S. vulgaris, S. lycopersicum, S. oleracea, T. aestivum, Z. mays
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BSA-conjugated, 11 amino acidslong synthetic peptide derived from a highly conserved sequence of Lhb1 proteins from angiosperms (monocots and dicots) and gymnosperms, including Arabidopsis thaliana Lhcb1.1 UniProt: P0CJ48-1, TAIR: AT1G29920, Lhcb1.2 UniProt: Q8VZ87-1, TAIR: AT1G29910, Lhcb1.3 (most expressed) UniProt: P04778-1, TAIR: AT1G2993, Lhcb1.4 UniProt: Q39142-1 , TAIR: AT2G34430, Lhcb1.5 UniProt: Q39141-1, TAIR: At2g34420
28 | 25 kDa for Arabidopsis thaliana
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10 µg of total protein from (1) Arabidopsis thaliana leaf, (2) Hordeum vulgare leaf, (3) Zea mays leaf, (4) Chlamydomonas reinhardtii total cell, (5) Spinacia oleracea total leaf, (6) Physcomitrella patens, (7) Solanum tuberosum total leaf, (8) Solanum esculentum total leaf, all extracted with Protein Extraction Buffer PEB (AS08 300) were separated on 4-12% NuPage (Invitrogen) LDS-PAGE and blotted 1h to PVDF. Blots were blocked immediately following transfer in 2-2.5 % blocking reagent in 20 mM Tris, 137 mM sodium chloride pH 7.6 with 0.1% (v/v) Tween-20 (TBS-T) for 1h at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1: 10 000 for 1h at room temperature with agitation. 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 room temperature with agitation. Blots were incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, recommended secondary antibody AS09 602) diluted to 1:25 000 in TBS-T for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min with chemiluminescent detection reagent according the manufacturers instructions. Images of the blots were obtained using a CCD imager (FluorSMax, Bio-Rad) and Quantity One software (Bio-Rad). Exposure time was 2 minutes.
Lhcb1 Protein is processed into mature form (Jansson 1999).
This product can be sold containing ProClin if requested
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. Lhcb1 is the most abundant chlorophyll a/b-binding protein in eukaryotic phototrophs and often is coded by several nuclear genes.
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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Shin et al. (2017), Complementation of a mutation in CpSRP43 causing partial truncation of light-harvesting chlorophyll antenna in Chlorella vulgaris. Sci Rep. 2017 Dec 20;7(1):17929. doi: 10.1038/s41598-017-18221-0.
Yang-Er Chen et al. (2017). Responses of photosystem II and antioxidative systems to high light and high temperature co-stress in wheat. J. of Exp. Botany, Volume 135, March 2017, Pages 45?55.
Mazur et al. (2016). Overlapping toxic effect of long term thallium exposure on white mustard (Sinapis alba L.) photosynthetic activity. BMC Plant Biol. 2016 Sep 2;16(1):191. doi: 10.1186/s12870-016-0883-4.
Kowalewska et al. (2016). Three-dimensional visualization of the internal plastid membrane network during runner bean chloroplast biogenesis. Dynamic model of the tubular-lamellar transformation. The Plant Cell March 21, 2016 tpc.01053.2015.
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Armbruster et al. (2014). Ion antiport accelerates photosynthetic acclimation in fluctuating light environments. Nat Commun. 2014 Nov 13;5:5439. doi: 10.1038/ncomms6439
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