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

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).

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.

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

The antibody recognizes bacterial GUS expressed in transgenic tobacco plants.

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

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

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

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