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Key Documents

CS0980

Sigma-Aldrich

Chitinase Assay Kit

sufficient for 100 multiwell tests

Synonyme(s) :

Chitinase Activity Detection Kit

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About This Item

Code UNSPSC :
12161503
Nomenclature NACRES :
NA.54

Utilisation

sufficient for 100 multiwell tests

Niveau de qualité

Rapport des absorbances

405 nm (Absorbance)

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

Description générale

The Chitinase Assay Kit is based on the enzymatic hydrolysis of chitinase substrates. The hydrolysis releases p-nitrophenol, which can be measured colormetrically at 405 nm.

Application

Chitinase Assay Kit has been used in screening chitinase activity of recombinant chitinase from yeast, Metschnikowia fructicola, bacterial endophyte 3A12 and Clostridium difficile spores.

The kit provides all the reagents required for efficient detection of chitinase activity in fungal and bacterial growth media, macrophage lysates, and purified enzyme preparations. In addition, the kit provides three different substrates for the detection of the various types of the chitinolytic activity:
  • 4-Nitrophenyl N,N′-diacetyl-β-D-chitobioside - substrate suitable for exochitinase activity detection (chitobiosidase activity)
  • 4-Nitrophenyl N-acetyl-β-D-glucosaminide - substrate suitable for exochitinase activity detection (β-N-acetylglucosaminidase activity)
4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose - substrate suitable for endochitinase activity detection

Actions biochimiques/physiologiques

Chitinase catalyzes the hydrolytic cleavage of the β-1→4-glycoside bond present in biopolymers of N-acetylglucosamine, primarily in chitin. Chitinases are widely distributed in living organisms and are found in fungi, bacteria, parasites, plants, and animals. They are classified in families based on amino acid sequence similarities.

The chitinolytic enzymes are also categorized based on their enzymatic action on chitin substrates. Endochitinases are defined as the enzymes catalyzing the random cleavage at internal points in the chitin chain. Exochitinases catalyze the progressive release of acetylchitobiose or N-acetylglucosamine from the non-reducing end of chitin, and are referred to as chitobiosidase and β-N-acetylglucosaminidase, respectively.

Chitinases perform different functions in different organisms. In bacteria, they are mainly involved in nutritional processes. In yeast and various fungi, these enzymes participate in morphogenesis. In animals and plants, chitinases primarily play a role in the defense of the organism against pathogen attack.

Remarque sur l'analyse

The kit assay is based on the enzymatic hydrolysis of chitinase substrates. This hydrolysis releases p-nitrophenol (4-nitrophenol), which upon ionization in basic pH can be measured colorimetrically at 405 nm.

Composants de kit seuls

Réf. du produit
Description

  • Assay Buffer 20 mL

  • 4-Nitrophenyl N-acetyl-β-D-glucosaminide 10 mg

  • 4-Nitrophenyl N,N′-diacetyl-β-D-chitobioside 5 mg

  • 4-Nitrophenyl β-D-N,N′N′′-triacetylchitotriose 1 mg

  • Chitinase from Trichoderma viride 1 mg

  • p-Nitrophenol Solution, 10 mM 1 mL

  • Sodium Carbonate 1 g

Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Carc. 2 - Eye Irrit. 2 - Resp. Sens. 1 - STOT RE 2 Oral

Organes cibles

Liver,Kidney

Code de la classe de stockage

10 - Combustible liquids


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Ahmed Akrem et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 3), 340-343 (2011-03-12)
A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the
E Patrick Fuerst et al.
Frontiers in plant science, 8, 2259-2259 (2018-02-08)
Seeds have well-established passive physical and chemical defense mechanisms that protect their food reserves from decay-inducing organisms and herbivores. However, there are few studies evaluating potential biochemical defenses of dormant seeds against pathogens. Caryopsis decay by the pathogenic Fusarium avenaceum
Functional characterization of Clostridium difficile spore coat proteins
Permpoonpattana P, et al.
Journal of Bacteriology, 195, 1492?1503-1492?1503 (2013)
The main virulence determinant of Yersinia entomophaga MH96 is a broad host range insect active, Toxin Complex
Hurst,M et al.
Journal of Bacteriology (2011)
Genes required for the anti-fungal activity of a bacterial endophyte isolated from a corn landrace grown continuously by subsistence farmers since 1000 BC
Shehata HR, et al.
Frontiers in Microbiology, 7, 1548-1548 (2016)

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