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G6920

Endo-β-galactosidase from Bacteroides fragilis

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

Synonim(y):

β-Galactosidase bacterial, Keratanase

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Gabaryty przesyłkiSKUDostępnośćCena netto
0.5 unit
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2790,00 zł

Informacje o tej pozycji

UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥140 units/mg protein
Recombinant:
expressed in E. coli

2790,00 zł


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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.[1] It was used for deglycosylation in glycoproteomics of the endothelial secretome of human endothelial cells.[2]

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.[3]

Physical form

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

Other Notes

One unit will release 1.0 μmole of reducing sugar from bovine corneal keratan sulfate per minute at 37 °C, pH 5.8.
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Ta pozycja
G5635G4155G7163
specific activity

≥140 units/mg protein

specific activity

≥500 units/mg protein

specific activity

≥500 units/mg protein (biuret)

specific activity

≥20 units/mg protein

form

buffered aqueous solution

form

lyophilized powder

form

aqueous glycerol suspension

form

buffered aqueous solution

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

expressed in E. coli

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

sterility

aseptically filled

sterility

-

sterility

-

sterility

-

mol wt

32 kDa

mol wt

465 kDa

mol wt

465 kDa

mol wt

80 kDa


Klasa składowania

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)



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Produkty

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

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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
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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.
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



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SKUNUMER GTIN
G6920-.5UN04061833642238

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