67138
β-(1→3)-D-Glucanase from Helix pomatia
≥0.2 U/mg
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10 MG
$140.00
50 MG
$553.00
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-927-3
MDL number:
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Product Name
β-(1→3)-D-Glucanase from Helix pomatia, ≥0.2 U/mg
biological source
Helix pomatia
form
powder
specific activity
≥0.2 U/mg
storage temp.
−20°C
Quality Level
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Related Categories
1 of 4
This Item | G7017 | G0762 | 77087 |
|---|---|---|---|
| biological source Helix pomatia | biological source Helix pomatia | biological source Helix pomatia | biological source - |
| specific activity ≥0.2 U/mg | specific activity ≥100,000 units/mL | specific activity ≥60,000 units/mL | specific activity ≥0.20 U/mg |
| form powder | form aqueous solution | form aqueous solution | form powder |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C |
| Quality Level 100 | Quality Level 300 | Quality Level 300 | Quality Level 100 |
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].
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
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Enrico Ragni et al.
Fungal genetics and biology : FG & B, 48(8), 793-805 (2011-05-24)
Cell wall biogenesis is a dynamic process relying on the coordinated activity of several extracellular enzymes. PHR1 is a pH-regulated gene of Candida albicans encoding a glycosylphosphatidylinositol-anchored β(1,3)-glucanosyltransferase of family GH72 which acts as a cell wall remodelling enzyme and
N P Sachivkina et al.
Bulletin of experimental biology and medicine, 149(6), 727-730 (2010-12-18)
Lyticase (a bacterial enzyme) was tested as a new antimycotic drug. Of all objects studied, Cellulomonas cellulans AC-870 strain proved to be most productive for this enzyme. A technology for lyticase isolation and purification was proposed. An experimental model of
The RabGAP proteins Gyp5p and Gyl1p recruit the BAR domain protein Rvs167p for polarized exocytosis.
Magali Prigent et al.
Traffic (Copenhagen, Denmark), 12(8), 1084-1097 (2011-05-11)
The Rab GTPase-activating proteins (GAP) Gyp5p and Gyl1p are involved in the control of polarized exocytosis at the small-bud stage in Saccharomyces cerevisiae. Both Gyp5p and Gyl1p interact with the N-Bin1/Amphiphysin/Rvs167 (BAR) domain protein Rvs167p, but the biological function of
Tomonari Tamashiro et al.
Glycoconjugate journal, 29(1), 77-85 (2011-12-27)
A carbohydrate-binding module from family 13 (CBM13), appended to the catalytic domain of endo-1,3-β-glucanase from Cellulosimicrobium cellulans, was overexpressed in E. coli, and its interactions with β-glucans, laminarin and laminarioligosaccharides, were analyzed using surface plasmon resonance biosensor and isothermal titration
María de Medina-Redondo et al.
PloS one, 5(11), e14046-e14046 (2010-12-03)
The formation of the cell wall in Schizosaccharomyces pombe requires the coordinated activity of enzymes involved in the biosynthesis and modification of β-glucans. The β(1,3)-glucan synthase complex synthesizes linear β(1,3)-glucans, which remain unorganized until they are cross-linked to other β(1,3)-glucans
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