Lhcb3 | LHCII type III chlorophyll a/b-binding protein

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

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 column.

AS01 002PRE | Lhcb3 | LHCII type III chlorophyll a/b-binding protein, pre-immune serum

AS01 003 | Anti-Lhcb2 | LHCII type II chlorophyll a/b-binding protein, rabbit antibodies

AS01 004 | Anti-Lhcb1 | LHCII type I chlorophyll a/b-binding protein, rabbit antibodies

Plant protein extraction buffer

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.