G5545
Anti-β-Glucuronidase (C-Terminal) antibody produced in rabbit
~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution
Synonyme(s) :
Anti-GUS
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About This Item
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Poids mol.
antigen 60 kDa
Espèces réactives
plant
Concentration
~1.5 mg/mL
Technique(s)
western blot: 1-2 μg/mL using purified GUS from E. coli
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Description générale
β-Glucuronidase (GUS) gene (also referred to as uidA) from Escherichia- coli, codes for a 60kDa protein.
Spécificité
Anit-β-Glucuronidase (C-Terminal) recognizes bacterial GUS expressed in transgenic tobacco plants.
The antibody recognizes bacterial GUS expressed in transgenic tobacco plants.
Immunogène
synthetic peptide corresponding to amino acids 589-603 at the C-terminus of E. coli GUS, conjugated to KLH.
Application
Detection of GUS by immunoblotting (60 kDa). Staining of the GUS band in immunoblotting is specifically inhibited by the immunizing GUS peptide (E. coli, amino acids 589-603).
Actions biochimiques/physiologiques
β-Glucuronidase (GUS) acts as a reporter gene for plant studies. Reporter genes are widely used for studying the expression of foreign genes in transformed plant tissues. GUS is an hydrolase that catalyzes the cleavage of a variety of β-glucuronide derivatives available for colorimetric, fluorometric and histochemical assays. GUS activity is easily assayed in vitro and can withstand fixation, enabling histochemical localization in cells and tissue sections. However, one of the major limitations of the gus reporter gene system is that the histochemical GUS assay system is destructive for the plant tissue, and therefore it is not suitable for direct visual selection of transformed plants.
Forme physique
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Notes préparatoires
The antibody is affinity-purified using the immunizing peptide immobilized on agarose.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Produit(s) apparenté(s)
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Transgenic Plants: Gene Constructs, Vector and Transformation Method
New Visions in Plant Science (2018)
Sebastian N W Hoernstein et al.
Molecular & cellular proteomics : MCP, 15(6), 1808-1822 (2016-04-14)
Protein arginylation is a posttranslational modification of both N-terminal amino acids of proteins and sidechain carboxylates and can be crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in moss, affects the low
Biolistic-mediated genetic transformation of cowpea (Vigna unguiculata) and stable Mendelian inheritance of transgenes
Ivo Nayche L, et al.
Plant Cell Reports, 27(9), 1475-1483 (2008)
Benjamin Dugdale et al.
The Plant cell, 25(7), 2429-2443 (2013-07-11)
In this study, we describe a novel protein production platform that provides both activation and amplification of transgene expression in planta. The In Plant Activation (INPACT) system is based on the replication machinery of tobacco yellow dwarf mastrevirus (TYDV) and
Mark D Harrison et al.
Plant biotechnology journal, 9(8), 884-896 (2011-03-02)
A major strategic goal in making ethanol from lignocellulosic biomass a cost-competitive liquid transport fuel is to reduce the cost of production of cellulolytic enzymes that hydrolyse lignocellulosic substrates to fermentable sugars. Current production systems for these enzymes, namely microbes
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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