67138
β-(1→3)-D-Glucanase from Helix pomatia
≥0.2 U/mg
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10 MG
$162.00
50 MG
$627.00
$162.00
Estimated to ship TODAYfromSAINT LOUIS
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biological source
Helix pomatia
form
powder
specific activity
≥0.2 U/mg
storage temp.
−20°C
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This Item | 45299 | G7017 | G0762 |
|---|---|---|---|
| biological source Helix pomatia | biological source - | biological source Helix pomatia | biological source Helix pomatia |
| specific activity ≥0.2 U/mg | specific activity ≥0.2 U/g | specific activity ≥100,000 units/mL | specific activity ≥60,000 units/mL |
| form powder | form lyophilized powder | form aqueous solution | form aqueous solution |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| Quality Level 100 | Quality Level 100 | Quality Level 300 | Quality Level 300 |
Application
β-(1→3)-D-Glucanase from Helix pomatia is used to digest β -1,3-glucan, which is a major component of cell walls. β-(1→3)-D-Glucanase from Helix pomatia has been used fto digest the cell walls of C. albicans [1].
Biochem/physiol Actions
Deletion of the C.albicans histidine kinase gene (CHK1) improves recognition by phagocytes through an increased exposure of cell wall b-1,3-glucans, which are readily digested by β-(1→3)-D-Glucanases [1].
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
One unit corresponds to the amount of enzyme which liberates 1 μmol of glucose from laminarin (Cat. No. 61340) per minute at pH 5.0 and 37 °C
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Nina Klippel et al.
Microbiology (Reading, England), 156(Pt 11), 3432-3444 (2010-08-07)
The pathogenic fungus Candida albicans is able to cover its most potent proinflammatory cell wall molecules, the β-glucans, underneath a dense mannan layer, so that the pathogen becomes partly invisible for immune cells such as phagocytes. As the C. albicans
Enrico Cabib et al.
Eukaryotic cell, 11(4), 388-400 (2012-03-01)
Previous results suggested that the chitin ring present at the yeast mother-bud neck, which is linked specifically to the nonreducing ends of β(1-3)glucan, may help to suppress cell wall growth at the neck by competing with β(1-6)glucan and thereby with
Marián Mazáň et al.
The Biochemical journal, 438(2), 275-282 (2011-06-10)
BGTs [β-(1,3)-glucanosyltransglycosylases; EC 2.4.1.-] of the GH72 (family 72 of glycosylhydrolases) are GPI (glycosylphosphatidylinositol)-anchored proteins that play an important role in the biogenesis of fungal cell walls. They randomly cleave glycosidic linkages in β-(1,3)-glucan chains and ligate the polysaccharide portions
Yoichi Tanabe et al.
Biochimica et biophysica acta, 1814(12), 1713-1719 (2011-10-08)
An endo-1,3-β-glucanase was purified from Tunicase®, a crude enzyme preparation from Cellulosimicrobium cellulans DK-1, and determined to be a 383-residue protein (Ala1-Leu383), comprising a catalytic domain of the glycoside hydrolase family 16 and a C-terminal carbohydrate-binding module family 13. The
Alexander M Zakharenko et al.
Carbohydrate research, 346(2), 243-252 (2010-12-15)
The retaining endo-1,3-β-d-glucanase (EC 3.2.1.39) was isolated from the crystalline styles of the commercially available Vietnamese edible mussel Perna viridis. It catalyzes hydrolysis of β-1,3-bonds in glucans and enables to catalyze a transglycosylation reaction. Resources of mass-spectrometry for analysis of
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