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Principaux documents

P2032

Sigma-Aldrich

Pepstatin A−Agarose

saline suspension

Synonyme(s) :

Pepstatin A resin

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About This Item

Numéro MDL:
MFCD00165221
Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

Source biologique

microbial (fermentation)
plant

Niveau de qualité

200

Forme

saline suspension

Technique(s)

affinity chromatography: suitable

Matrice

cross-linked 4% beaded agarose

Activation de la matrice

cyanogen bromide

Fixation de matrice

carboxyl

Espaceur de matrice

9 atoms

Capacité

20-40 mg/mL binding capacity (pepsin)

Adéquation

suitable for chromatography

Température de stockage

2-8°C

Application

Pepstatin A-agarose is used in protein chromatography, affinity chromatography and specialty resins. Pepstatin A-agarose has been used to characterize three chitosanase isozymes isolated from a commercial crude porcine pepsin preparation.

Forme physique

Suspension in 0.5 M NaCl containing preservative

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

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P Geldhof et al.
International journal for parasitology, 33(2), 129-136 (2003-03-14)
A pepstatin A-agarose column was used in an attempt to purify a previously described antibody-degrading aspartyl proteinase from excretory-secretory material from the L4 and the adult stages of the bovine abomasal nematode Ostertagia ostertagi. However, no aspartyl proteinase activity was
N Hiraiwa et al.
European journal of biochemistry, 246(1), 133-141 (1997-05-15)
To understand the mechanism of the maturation of various proteins in protein-storage vacuoles, we purified a 48-kDa aspartic endopeptidase composed of 32-kDa and 16-kDa subunits from castor bean. Immunocytochemical and cell fractionation analyses of the endosperm of maturing castor bean
C J Morrison et al.
Journal of general microbiology, 139 Pt 6, 1177-1186 (1993-06-01)
Aspartyl proteinase (AP) is an extracellular enzyme of Candida albicans implicated as a pathogenic factor. Previous reports on the purification and characterization of AP suggested that a single DEAE-Sephadex chromatographic step was sufficient for the removal of extraneous proteins and
Liliana Rojo et al.
Marine biotechnology (New York, N.Y.), 12(6), 696-707 (2010-02-20)
Acid digestive proteinases were studied in the gastric fluids of two species of clawed lobster (Homarus americanus and Homarus gammarus). An active protein was identified in both species as aspartic proteinase by specific inhibition with pepstatin A. It was confirmed
O Carnevali et al.
Biology of reproduction, 60(1), 140-146 (1998-12-22)
Oocyte growth within the follicle is preponderantly due to the accumulation of hepatically derived yolk protein (vitellogenin, VTG) by receptor-mediated endocytosis; once in the oocyte, VTG is partially processed and stored in yolk globules. In some pelagic egg-laying marine teleosts
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