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EPSP synthase | 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic

265 €
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AS14 2782 | clonality: polyclonal | host: rabbit | reactivity: Arabidopsis thaliana, di and monocots

PRODUCT INFORMATION IN PDF

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AS14 2782

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product information
Background EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic) is an enzyme (EC:2.5.1.19)which is involved in glyphosate metabolic process. Localized in chloroplast stroma. Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. Alternative name: 5-enolpyruvylshikimate-3-phosphate synthase.
Immunogen

KLH-conjugated peptide, derived from Arabidopsis thaliana EPSP synthase, UniProt: P05466 TAIR:At2g45300

Host Rabbit
Clonality Polyclonal
Clone
Purity Serum
Format Lyophilized
Quantity 50 ĩl
Reconstitution For reconstitution add 50 ĩl of sterile water.
Storage

store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Tested applications western blot (WB)
Related products

AS16 3119 | anti-EPSP synthase | 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic, rabbit antibodies

Recommended secondary antibody for ECL detection

Plant protein extraction buffer

Secondary antibodies

Additional information
application information
Recommended dilution

1: 1000 for ECL (WB)

Expected | apparent MW

55 kDa

Confirmed reactivity

Arabidopsis thaliana

Predicted reactivity
Not reactive in
Additional information
Selected references to be added when available, antibody released in January 2015

application example

 
western 0.5 µg of purified Arabidopsis thaliana EPSPS was separated on 10 % SDS-PAGE and blotted 2h to nitrocellulose Hibond ECLmembrane (GE Healthcare) using semi-dry or tank transfer. Blots were blocked with for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody in TBS-T with (0.1 % Tween 20) at a dilution of 1: 1 000 for 1h at RT with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 2 times for 5 min in TBS-T at RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from Agrisera AS09 602) diluted to 1: 20 000 in for 1h at RT with agitation. The blot was washed as above and developed for 5 min with ECL according to the manufacturer's instructions. Protein detection was done by Image Quant LAS4000 (GE-Health Care) digital imager system with exposure time was of 5 minutes.

Recombinant Arabidopsis thaliana EPSPS protein (aka 3-phosphoshikimate 1-carboxyvinyltransferase) used in the assay was identified by LCMS.

Courtesy of Dr. Altanbadralt Sharkhuu, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia

western
50 µg of total protein from shoots of 18 d old Arabidopsis thaliana were extracted with buffer (125 mM Tris-HCl ph6.8; 12% SDS; 10% glycerol, 22% b-mercaptoethanol; 0.001% bromophenol blue) were separated on % SDS-PAGE and blotted 3h to nitrocellulose membrane using tank transfer. Blots were blocked with TBST with 5% skim milk for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody (Rabbit-EPSPS) at a dilution of 1: 1 000 for over night at 4 C 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 RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from Agrisera AS09 602) diluted to 1:20 000 in for 1h at RT with agitation. The blot was washed as above and developed for 5 min with ECL according to the manufacturer's instructions. Detection was done by Image Quant LAS 4000 (GE-Health Care). Exposure time was 2 min.

Courtesy of Dr. Altanbadralt Sharkhuu, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia

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