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Anti-BG1 | Beta-glucosidase 1
Product no: AS20 4419
AS20 4419 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana
369
€
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- Product Info
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Immunogen: Purified recombinant BG1 of Arabidopsis thaliana, residues 27-528 with a His6-thioredoxin tagged, UniProt: Q9SE50, TAIR: At1g52400 Host: Rabbit Clonality: Polyclonal Purity: Total IgG. Protein A purified in PBS, 50% glycerol. Filter sterilized. Format: Liquid at 2 mg/ml. Quantity: 200 µg Storage: Store at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube. Tested applications: Immunolocalization (IL) using electron microscopy, Western blot (WB) Recommended dilution: 1: 1000 (IL), 1: 2000 - 1: 4000 (WB) Expected | apparent MW: 60.4 | 60 kDa - Reactivity
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Confirmed reactivity: Arabidopsis thaliana Predicted reactivity: Species of your interest not listed? Contact us Not reactive in: No confirmed exceptions from predicted reactivity are currently known - Application Examples
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Arabidopsis thaliana 7 day-old seedling were freshly extracted with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE and denatured with 4X SDS buffer at 95°C for 5 min. Sample was separated on a 15-20 % SDS-PAGE gradient gel and blotted using wet transfer to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1000 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
Accumulation of BG1 in locally wounded cotyledons of both GFPh plants (wild-type with GFP-fused with ER-retention signal) and nai1 mutant but not visible in bglu18 mutant.
Arabidopsis thaliana 12 day-old cotyledons were freshly extracted with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE and denatured with 4X SDS buffer at 95°C for 5 min. Sample was separated on 12.5 % SDS-PAGE and blotted using wet transfer to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 2000 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
U - unwounded; L- locally wounded; S- systemically wounded - Background
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Background: BG1 (Beta-glucosidase 1) hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level. Localised to ER lumen.Alternative names: AtBG1, Beta-glucosidase 18, Beta-glucosidase homolog 1. - Product Citations
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Selected references: Ogasawara et al. (2009). Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases. Plant Cell Physiol. 2009 Mar;50(3):480-8. doi: 10.1093/pcp/pcp007. - Protocols
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Agrisera Western Blot protocol and video tutorials
Protocols to work with plant and algal protein extracts
Agrisera Educational Posters Collection - Reviews:
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