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Key Documents

G6920

Sigma-Aldrich

Endo-β-galactosidase from Bacteroides fragilis

recombinant, expressed in E. coli, ≥140 units/mg protein, buffered aqueous solution

Synonym(s):

β-Galactosidase bacterial, Keratanase

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

conjugate

(Glucosaminoglycan)

sterility

aseptically filled

form

buffered aqueous solution

specific activity

≥140 units/mg protein

mol wt

32 kDa

storage temp.

2-8°C

Application

Endo-β-galactosidase was used in fractional protein isolation. It was used for deglycosylation in glycoproteomics of the endothelial secretome of human endothelial cells.

Biochem/physiol Actions

Internal β(1-4) galactose linkages in unbranched, repeating poly-Nacetyllactosamine [GlcNAc β(1-3)Gal β (1-4)] structures are the preferred substrate.

Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may reduce or completely inhibit cleavage. Sulfation of C-6 on galactose will block cleavage. Oligosaccharides of the neolacto-group are cleaved at greatly reduced rates depending on the deviation from the preferred substrate. For example, Gal β(1-3)GlcNAc β(1-3) Gal β(1-4)Glc is cleaved at 5X10-5 the rate of keratan sulfate

β-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose. It also catalyses the transglycosylation of glucose into allolactose, the inducer of β-galactosidase, in a feedback loop.

Unit Definition

One unit will release 1.0 μmole of reducing sugar from bovine corneal keratan sulfate per minute at 37 °C, pH 5.8.

Physical form

Aseptically filled solution in 20 mM Tris-HCl, pH 7.5

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Xiaoke Yin et al.
Molecular & cellular proteomics : MCP, 12(4), 956-978 (2013-01-25)
Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication. In this study, human umbilical vein endothelial cells were kept in serum-free
Maria Vistnes et al.
PloS one, 9(3), e89621-e89621 (2014-03-07)
We hypothesized that cleavage of the extracellular matrix (ECM) proteoglycans versican and aggrecan by ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs) proteases, which contributes to stress-induced ECM-reorganization in atherogenesis and osteoarthritis, also play a role in heart failure development.
Salvatore Santamaria et al.
Scientific reports, 11(1), 949-949 (2021-01-15)
ADAMTS-5 is a major protease involved in the turnover of proteoglycans such as aggrecan and versican. Dysregulated aggrecanase activity of ADAMTS-5 has been directly linked to the etiology of osteoarthritis (OA). For this reason, ADAMTS-5 is a pharmaceutical target for
Xiaoke Yin 殷晓科 et al.
Arteriosclerosis, thrombosis, and vascular biology, 39(9), 1859-1873 (2019-07-19)
Marfan syndrome (MFS) is caused by mutations in FBN1 (fibrillin-1), an extracellular matrix (ECM) component, which is modified post-translationally by glycosylation. This study aimed to characterize the glycoproteome of the aortic ECM from patients with MFS and relate it to
Salvatore Santamaria et al.
Scientific reports, 9(1), 10914-10914 (2019-07-31)
ADAMTS (A Disintegrin-like and Metalloproteinase domain with Thrombospondin type 1 Motif)-1, -4 and -5 share the abilities to cleave large aggregating proteoglycans including versican and aggrecan. These activities are highly relevant to cardiovascular disease and osteoarthritis and during development. Here

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