Invitrogen™ X-Gal (5-Bromo-4-Chloro-3-Indolyl β-D-Galactopyranoside)

Description

Substrate yields a dark blue precipitate at the site of enzymatic activity. X-Gal is useful for numerous histochemical and molecular biology applications, including detection of lacZ activity in cells and tissues. In contrast to β-glucuronidase as a gene marker, β-galactosidase can be fixed in cells and tissues with glutaraldehyde without loss of activity and detected with high resolution using X-Gal.

Additional Information About Glycosidase Enzymes
Glycosidase enzymes exhibit very high selectivity for hydrolysis of their preferred sugars. For example, β-galactosidase rapidly hydrolyzes β-D-galactopyranosides but usually does not hydrolyze either the anomeric α-D-galactopyranosides or the isomeric β-D-glucopyranosides. Endogenous glycosidase activity is frequently used to characterize strains of microorganisms and to selectively label organelles of mammalian cells; defects in glycosidase activity are characteristic of several diseases.

In addition, glycosidases are important reporter gene markers. Specifically, lacZ, which encodes β-galactosidase, is extensively used as a reporter gene in animals and yeast, whereas the β-glucuronidase (GUS) gene is a popular reporter gene in plants. Glycosidase substrates are also used in conjunction with glycosidase-conjugated secondary detection reagents in immunohistochemical techniques and enzyme-linked immunosorbent assays (ELISAs).

• Chromogenic substrate
• Cell permeant
• β-galactosidase activity can still be detected using X-Gal after fixation

Beta-Galactosidase Assays, Cell Analysis, Cellular Imaging, Cloning, Enzyme and Protein Activity Assays, Glycosidase, Neuraminidase, and Related Enzyme Activity, IHC Staining and Detection, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Proteins, Expression, Isolation and Analysis, Reporter Assays, Transformation

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Shipping Condition: Room Temperature