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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, 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
William Mark Erwin et al.
Arthritis research & therapy, 17, 240-240 (2015-09-06)
In the present study, we sought to quantify and contrast the secretome and biomechanical properties of the non-chondrodystrophic (NCD) and chondrodystrophic (CD) canine intervertebral disc (IVD) nucleus pulposus (NP). We used iTRAQ proteomic methods to quantify the secretome of both
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

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Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

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