PR-2 | GLU I | Class I beta-1,3-glucanase
AS07 208 | Clonality: Polyclonal | Host: Rabbit | Reactivity: N. benthamiana, N. clevilandii, N. tabacum, Phalenopsis, P.abies, S.lycopersicum, S. tuberosum, V. vinifera | compartment marker of vacuolar contents

Data sheet | Product citations | Protocols | Customer reviews |
Product Information
Purified tobacco class I, basic ß-1,3-glucanase. Purified GLU I consists of a mixture of closely related polypeptides encoded by a family of GLU I genes comprising GLA B5APL3 derived from the sylvestris ancestor of tobacco, GLB P27666 derived from the tomentosiformis ancestor of tobacco and homeologous recombinants (Sperisen et al., 1991). Mature GLU I is processed from a pre-pro-polypeptide (Shinshi et al., 1988).
37 | 33 kDa
Reactivity
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Arabidopsis thaliana
Application examples
Application example
Detection of tobacco tobacco class I ß 1,3 – glucanase in ng loaded per respective well using anti- tobacco class I ß 1,3 – glucanase antibodies. Primary antibodies have been used at 8 µg/ml.
Additional information
For more details on immunolocalization, please referr to Keefe et al (1990). Plant 182: 43-51.
This antibody can be used as a marker of vacuolar contents Keefe et al. (1990). The effect of ethylene on the cell-type-specific and intracellular localization of β-1,3-glucanase and chitinase in tobacco leave. Plant 182: 43-51.
Important note: for blocking 5 % skim milk in PBS without Ca++ should be used.
This antibody is purified by affinity chromarography on Portein G.
Background
Pathogenesis-related (PR) proteins, are induced in response to the infection of plants with microbial pathogens. Combinations of glucanase I and chitinase I are potent inhibitors of fungal growth in vitro however precise mechanism of that is still not known. Glucanase I and chitinase I contribute to defense against fungal infection and are currently used as markers for innate immunity, and in particular the ethylene/jasmonate signalling pathway in pathogenesis. Alternative names of the protein: basic beta-1,3-glucanase
Product citations
Colman et al. (2019). Chitosan microparticles improve tomato seedling biomass and modulate hormonal, redox and defense pathways. Plant Physiology and Biochemistry. Volume 143, October 2019, Pages 203-211.
Martin-Saladana et al. (2018). Salicylic acid loaded chitosan microparticles applied to lettuce seedlings: Recycling shrimp fishing industry waste. Carbohydrate Polymers Volume 200, 15 November 2018, Pages 321-331.
Wang et al. (2014). Elicitation of Hypersensitive Responses in Nicotiana glutinosa by the Suppressor of RNA Silencing Protein P0 from Poleroviruses. Mol Plant Pathol. 2014 Sep 4. doi: 10.1111/mpp.12201.
Huey-wen et al. (2014). Harpin Protein, an Elicitor of Disease Resistance, Acts as a Growth Promoter in Phalaenopsis Orchids. Journal of Plant Growth Regulation May 2014.
Munger et al. (2012). Beneficial ‘unintended effects’ of a cereal cystatin in transgenic lines of potato, Solanum tuberosum. BMC Plant Biol. 2012 Nov 1;12:198. doi: 10.1186/1471-2229-12-198.
Related products: PR-2 | GLU I | Class I beta-1,3-glucanase
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