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Merck
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Key Documents

P2032

Sigma-Aldrich

Pepstatin A−Agarose

saline suspension

Sinónimos:

Pepstatin A resin

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About This Item

Número MDL:
MFCD00165221
Código UNSPSC:
41106500
NACRES:
NA.56

origen biológico

microbial (fermentation)
plant

formulario

saline suspension

técnicas

affinity chromatography: suitable

matriz

cross-linked 4% beaded agarose

activación de la matriz

cyanogen bromide

unión a la matriz

carboxyl

espaciador de matriz

9 atoms

capacidad

20-40 mg/mL binding capacity (pepsin)

idoneidad

suitable for chromatography

temp. de almacenamiento

2-8°C

Aplicación

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.

Forma física

Suspension in 0.5 M NaCl containing preservative

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (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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