other

Anti-GAL Beta galactosidase

AS20 4515

200 µg

253 USD

Anti-GAL Beta galactosidase

Primary antibody

Rabbit

Polyclonal

200 µg

253 USD

P42212

Beta-galactosidase is an exoglycosidase which hydrolyzes the -glycosidic bond formed between agalactose and its organic moiety. It may also cleave fucosides and arabinosides but with much lower efficiency. It is an essential enzyme in the human body. Deficiencies in the protein can result ingalactosialidosis or Morquio B syndrome. In E. coli , the gene of -galactosidase, the lacZ gene, is present as part of the inducible system lac operon which is activated in the presence of lactose when glucose level is low. It is commonly used in molecular biology as a reporter marker to monitor gene expression. It also exhibits a phenomenon called -complementation which forms the basis for the blue/white screening of recombinant clones. This enzyme can be split in two peptides, LacZ and LacZ , neither of which is active by itself but when both are present together, spontaneously reassemble into a functional enzyme. This property is exploited in many cloning vectors where the presence of the lacZ gene in a plasmid can complement in trans another mutant gene encoding the LacZ in specific laboratory strains of E. coli . However, when DNA fragments are inserted in the vector, the production of LacZ is disrupted, the cells therefore show no -galactosidase activity. The presence or absence of an active -galactosidase may be detected by X-gal, which produces a characteristic blue dye when cleaved by -galactosidase, thereby providing an easy means of distinguishing the presence or absence of cloned product in a plasmid. E. coli -Galactosidase consists of 1,024 amino acids with molecular mass of 116 kDa and functional form is a homotetramer.

Beta galactosidase (E.coli) and beta galactosidase tagged proteins

Beta-galactosidase is an exoglycosidase which hydrolyzes the -glycosidic bond formed between agalactose and its organic moiety. It may also cleave fucosides and arabinosides but with much lower efficiency. It is an essential enzyme in the human body. Deficiencies in the protein can result ingalactosialidosis or Morquio B syndrome. In E. coli , the gene of -galactosidase, the lacZ gene, is present as part of the inducible system lac operon which is activated in the presence of lactose when glucose level is low. It is commonly used in molecular biology as a reporter marker to monitor gene expression. It also exhibits a phenomenon called -complementation which forms the basis for the blue/white screening of recombinant clones. This enzyme can be split in two peptides, LacZ and LacZ , neither of which is active by itself but when both are present together, spontaneously reassemble into a functional enzyme. This property is exploited in many cloning vectors where the presence of the lacZ gene in a plasmid can complement in trans another mutant gene encoding the LacZ in specific laboratory strains of E. coli . However, when DNA fragments are inserted in the vector, the production of LacZ is disrupted, the cells therefore show no -galactosidase activity. The presence or absence of an active -galactosidase may be detected by X-gal, which produces a characteristic blue dye when cleaved by -galactosidase, thereby providing an easy means of distinguishing the presence or absence of cloned product in a plasmid. E. coli -Galactosidase consists of 1,024 amino acids with molecular mass of 116 kDa and functional form is a homotetramer.

Full length Beta galactosidase from E.coli UniProt: B7UJI9

Total IgG. Protein A purified in PBS, 50 % glycerol, filter sterilized.

ELISA (ELISA), Immunofluorescence (IF), Immunoprecipitation (IP), Western blot (WB)

ELISA (ELISA), Immunofluorescence (IF), Immunoprecipitation (IP), Western blot (WB)

Store at -20°C, Avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube. , Do not store this antibody below -20°C