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P2032

Sigma-Aldrich

Pepstatin A−Agarose

saline suspension

Synonym(s):

Pepstatin A resin

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5 ML
€765.00
10 ML
€880.00
25 ML
€1,780.00

€765.00


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5 ML
€765.00
10 ML
€880.00
25 ML
€1,780.00

About This Item

MDL number:
UNSPSC Code:
41106500
NACRES:
NA.56

€765.00


Please contact Customer Service for Availability

biological source

microbial (fermentation)
plant

form

saline suspension

technique(s)

affinity chromatography: suitable

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

carboxyl

matrix spacer

9 atoms

capacity

20-40 mg/mL binding capacity (pepsin)

suitability

suitable for chromatography

storage temp.

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.

Physical form

Suspension in 0.5 M NaCl containing preservative

Storage Class Code

10 - Combustible liquids

WGK

WGK 3


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H S Kim et al.
Journal of immunology (Baltimore, Md. : 1950), 165(6), 3268-3274 (2000-09-07)
The intestinal epithelium forms a first line of innate host defense by secretion of proteins with antimicrobial activity against microbial infection. Despite the extensive studies on the antimicrobial host defense in many gastrointestinal tracts, little is known about the antimicrobial
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
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
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
Jacob W Ufberg et al.
The American journal of emergency medicine, 22(7), 612-614 (2005-01-25)
Aspiration of gastric contents by endotracheally intubated patients is associated with significant morbidity and mortality. Previous studies suggest that pepsin in tracheal aspirates may be a valuable marker of occult aspiration. We sought to show the sensitivity and specificity of

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