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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:
Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

Source biologique

microbial (fermentation)
plant

Niveau de qualité

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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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
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
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
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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