Description
Key facts
Purity:>97% HPLC,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:IASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P00722,
Animal free:No,
Carrier free:No,
Species:Escherichia coli K-12,
Storage buffer:Constituents: 10% Sucrose, 0.42% Tripotassium orthophosphate
Product details:
Beta Galactosidase was prepared chromatographically. This product has been sterile filtered. Beta Galactosidase is used as a control in beta-galactosidase based immunological assays.
Beta-galactosidase, also called beta-gal or Beta-gal, is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Lactase is often confused as an alternative name for Beta-galactosidase, but it is simply a sub-class of Beta-galactosidase. Beta-galactosidase is an exoglycosidase which hydrolyzes the Beta-glycosidic bond formed between a galactose 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 in galactosialidosis or Morquio B syndrome. In E. coli, the gene of Beta-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 alpha-complementation which forms the basis for the blue/white screening of recombinant clones. This enzyme can be split in two peptides, LacZ-alpha and LacZ-omega 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-alpha gene in a plasmid can complement in trans another mutant gene encoding the LacZ-omega in specific laboratory strains of E. coli. However, when DNA fragments are inserted in the vector, the production of LacZ-alpha is disrupted, the cells therefore show no Beta-galactosidase activity. The presence or absence of an active Beta-galactosidase may be detected by X-gal, which produces a characteristic blue dye when cleaved by Beta-galactosidase, thereby providing an easy means of distinguishing the presence or absence of cloned product in a plasmid.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Beta Galactosidase often called "β-gal" "b-galactosidase" or "b-gal" serves as an important enzyme that hydrolyzes β-galactosides into monosaccharides. It breaks down lactose into glucose and galactose which are easier to absorb. Beta-galactosidase expresses in many organisms such as *E. coli* where it is a well-known component of the lac operon. Its molecular weight in *E. coli* is approximately 116 kDa. The enzyme also appears in human tissues but is synthesized and regulated differently compared to bacterial systems.
Biological function summary
This enzyme is involved in the metabolism of galactose a critical aspect of cellular energy production. It can participate in various metabolic pathways converting complex carbohydrates into simpler sugars. In bacteria beta-galactosidase belongs to a protein complex controlled by the lac operon regulating lactose metabolism. In humans the enzyme takes part in lysosomal functions contributing to the degradation of glycoproteins and glycolipids therefore supporting normal cellular processes.
Pathways
Beta-galactosidase plays an important role in the lactose metabolism pathway. In *E. coli* it coheres with the enzymes of the lac system like lactose permease and transacetylase to facilitate lactose utilization. In human biology it participates in the lysosomal degradation pathway. Its function is associated with proteins such as galactosylceramidase which also break down galactolipids demonstrating its interaction in broader metabolic networks.
Deficiencies or malfunctions in beta-galactosidase lead to metabolic conditions like Galactosialidosis and Morquio syndrome Type B. These are lysosomal storage disorders caused by a lack of enzyme activity leading to accumulation of partially degraded macromolecules. The enzyme's impaired function connects with other proteins such as protective protein cathepsin A in the case of Galactosialidosis causing complex clinical symptoms through disrupted protein interactions and pathways.
