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P2032

Sigma-Aldrich

Pepstatin A−Agarose

saline suspension

Synonym(s):

Pepstatin A resin

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About This Item

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

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


Certificates of Analysis (COA)

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Madanan Madathiparambil Gopalakrishnan et al.
The Biochemical journal, 383(Pt. 3), 507-515 (2004-07-17)
Before delivery to endosomes, portions of proCD (procathepsin D) and proSAP (prosaposin) are assembled into complexes. We demonstrate that such complexes are also present in secretions of cultured cells. To study the formation and properties of the complexes, we purified
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
F Canduri et al.
Biochemistry and molecular biology international, 45(4), 797-803 (1998-08-26)
Cathepsin D, a lysosomal aspartic protease, has been purified from porcine liver using a combination of pepstatin-A agarose and Affi-Gel Blue affinity chromatography, followed by size-exclusion chromatography. The purified protein consists of two polypeptide chains of 15 and 30 kDa
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

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