beta-Galactosidase Reporter Detection Kits

&#945-Galactosidase from green coffee beans is encoded by the GLA gene. Application &#945-Galactosidase from green coffee beans has been used to assess the specificity of anti- &#945-Galactosidase antibodies.

&#945-Galactosidase from green coffee beans is encoded by the GLA gene. Application &#945-Galactosidase from green coffee beans has been used to assess the specificity of anti- &#945-Galactosidase antibodies.

&#945-Galactosidase from green coffee beans is encoded by the GLA gene. Application &#945-Galactosidase from green coffee beans has been used to assess the specificity of anti- &#945-Galactosidase antibodies.

Recombinant &#9451-3,6-galactosidase expressed in E. coli .

Specificity Galactosidase, alpha. Immunogen Synthetic peptides from human galactosidase, alpha.

Specificity Recognizes Beta-Galactosidase (E. coli).

The previously assigned protein identifier P16279 has been merged into P16278. Full details can be found on the UniProt database.

&#946 Galactosidase, also known as Beta-galactosidase, Beta-gal, LacZ, or Lactase, and encoded by the gene lacZ, is the enzyme in bacteria that hydrolyzes galactosides (sugars chains containing galactose) in to monosaccharides. &#946

&#946-Galactosidase is present in bacteria, fungi, yeast and animal organs. It is also found in fruits, such as apples, almonds and apricots.

HOST SPECIES: Chicken CLONALITY: Polyclonal TESTED APPLICATIONS: E, WB APPLICATIONS: beta-gal antibody can be used for detection of beta-gal by Western blot at 1 &#956g/mL. SPECIES REACTIVITY: Bacteria IMMUNOGEN: beta-gal antibody was raised

Application &#946-Galactosidase from bovine testes was used for coupling to Sepharose. Biochem/physiol Actions &#946-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose.

Application &#946-Galactosidase from bovine testes was used for coupling to Sepharose. Biochem/physiol Actions &#946-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose.