P2032
Pepstatin A−Agarose
saline suspension
Synonym(s):
Pepstatin A resin
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About This Item
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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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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
Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I.
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
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
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
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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