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
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 23(9), 3007-3019 (2009-04-22)
Hookworms digest hemoglobin from erythrocytes via a proteolytic cascade that begins with the aspartic protease, APR-1. Ac-APR-1 from the dog hookworm, Ancylostoma caninum, protects dogs against hookworm infection via antibodies that neutralize enzymatic activity and interrupt blood-feeding. Toward developing a
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
Theriogenology, 63(5), 1481-1503 (2005-02-24)
The pregnancy-associated glycoproteins (PAGs) are a large gene family expressed in trophoblast cells of ruminant ungulates. The detection of PAGs (more specifically, PAG-1) in maternal serum has served as the basis for pregnancy detection in cattle. Unfortunately, PAG-1 and/or antigenically-related
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