Skip to Content
Merck
All Photos(1)

Key Documents

67138

Sigma-Aldrich

β-(1→3)-D-Glucanase from Helix pomatia

≥0.2 U/mg

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

Helix pomatia

form

powder

specific activity

≥0.2 U/mg

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

Application

β-(1→3)-D-Glucanase from 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 .

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 .

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Feng Duan et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 27(7), 1092-1099 (2011-10-25)
In order to explore the influence of reaction temperature on the product composition, the effect of continuous temperature change (22 degrees C-60 degrees C, +/-0.1 degree C) on hydrolysis of yeast beta-glucan by endo-beta-1,3-glucanase was determined by using self-developed Biochem-temperature
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
Poonam Gautam et al.
Mycopathologia, 172(5), 331-346 (2011-07-15)
Artemisinin, an antimalarial drug, and its derivatives are reported to have antifungal activity against some fungi. We report its antifungal activity against Aspergillus fumigatus (A. fumigatus), a pathogenic filamentous fungus responsible for allergic and invasive aspergillosis in humans, and its
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service