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Merck

G5545

Sigma-Aldrich

Anti-β-Glucuronidase (C-Terminal) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(e):

Anti-GUS

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 60 kDa

Speziesreaktivität

plant

Konzentration

~1.5 mg/mL

Methode(n)

western blot: 1-2 μg/mL using purified GUS from E. coli

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Allgemeine Beschreibung

β-Glucuronidase (GUS) gene (also referred to as uidA) from Escherichia- coli, codes for a 60kDa protein.

Spezifität

Anit-β-Glucuronidase (C-Terminal) recognizes bacterial GUS expressed in transgenic tobacco plants.
The antibody recognizes bacterial GUS expressed in transgenic tobacco plants.

Immunogen

synthetic peptide corresponding to amino acids 589-603 at the C-terminus of E. coli GUS, conjugated to KLH.

Anwendung

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).

Biochem./physiol. Wirkung

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.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Angaben zur Herstellung

The antibody is affinity-purified using the immunizing peptide immobilized on agarose.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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
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)
Transgenic Plants: Gene Constructs, Vector and Transformation Method
New Visions in Plant Science (2018)

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