P5431
Pectolyase from Aspergillus japonicus
aseptically filled, lyophilized powder, ≥2 units/mg solid
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Numero MDL:
Codice UNSPSC:
12352204
Sterilità
aseptically filled
Forma fisica
lyophilized powder
Attività specifica
≥2 units/mg solid
Temperatura di conservazione
2-8°C
Cerchi prodotti simili? Visita Guida al confronto tra prodotti
Applicazioni
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Altre note
Reported to contain two types of pectinase, endopolygalacturonase (EC3.2.1.15), endopectin lyase (EC4.2.2.10) and a maceration stimulating factor.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Definizione di unità
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 5.5 at 25 °C.
Stato fisico
Lyophilized powder containing lactose
Nota sulla preparazione
Prepared from P 3026
Prodotto comparabile
N° Catalogo
Descrizione
Determinazione del prezzo
Codice della classe di stoccaggio
13 - Non Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
Claudia Schinke et al.
International microbiology : the official journal of the Spanish Society for Microbiology, 15(1), 1-7 (2012-07-28)
Macrophomina phaseolina, phylum Ascomycota, is a phytopathogenic fungus distributed worldwide in hot dry areas. There are few studies on its secreted lipases and none on its colony radial growth rate, an indicator of fungal ability to use nutrients for growth
Shashi Kant et al.
Protein expression and purification, 87(1), 11-16 (2012-10-17)
Polygalacturonases are the pectinolytic enzymes that catalyze the hydrolytic cleavage of the polygalacturonic acid chain. In the present study, polygalacturonase from Aspergillus niger (MTCC 3323) was purified. The enzyme precipitated with 60% ethanol resulted in 1.68-fold purification. The enzyme was
Paulo Roberto Adalberto et al.
The Analyst, 137(20), 4855-4859 (2012-09-05)
Polygalacturonases (EC 3.2.1.15) hydrolyze the α-1,4-glycosidic linkages in polygalacturonic acid chains. The interest on specific inhibitors of pectinase and the versatility of magnetic support for enzyme immobilization endorsed the preparation of an immobilized enzyme reactor (IMER). This work presents the
S S Ahmed et al.
Genetics and molecular research : GMR, 11(3), 3091-3104 (2012-09-26)
Molecular chaperones of plasmid pBI121 carrying CaMV35S promoter and a nucleotide sequence of plasmid pBI221 were inserted into plasmid pCAMBIA2300 to construct an intermediate vector: pVBG2307. This novel vector pVBG2307 contains a greatly expanded multiple cloning site with an adjacent
Peerapat Roongsattham et al.
BMC plant biology, 12, 150-150 (2012-08-28)
Cell separation that occurs during fleshy fruit abscission and dry fruit dehiscence facilitates seed dispersal, the final stage of plant reproductive development. While our understanding of the evolutionary context of cell separation is limited mainly to the eudicot model systems
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.