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G5545

Sigma-Aldrich

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

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

Synonym(s):

Anti-GUS

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 60 kDa

species reactivity

plant

concentration

~1.5 mg/mL

technique(s)

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

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

Specificity

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.

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).

Biochem/physiol Actions

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.

Physical form

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

Preparation Note

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (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

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