P0525000
Pepsin
powder, European Pharmacopoeia (EP) Reference Standard
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About This Item
Recommended Products
grade
pharmaceutical primary standard
form
powder
manufacturer/tradename
EDQM
application(s)
pharmaceutical (small molecule)
format
neat
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General description
Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep.
Application
Pepsin EP Reference standard, intended for use in laboratory tests only as specifically prescribed in the European Pharmacopoeia.
Packaging
The product is delivered as supplied by the issuing Pharmacopoeia. For the current unit quantity, please visit the EDQM reference substance catalogue.
Other Notes
Sales restrictions may apply.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 1
Flash Point(C)
Not applicable
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Chest, 143(5), 1407-1413 (2012-11-03)
Airway pepsin has been increasingly used as a potentially sensitive and quantifiable biomarker for gastric-to-pulmonary aspiration, despite lack of validation in normal control subjects. This study attempts to define normal levels of airway pepsin in adults and distinguish between pepsin
European review for medical and pharmacological sciences, 17(11), 1427-1437 (2013-06-19)
Recently, type II collagen (CII) was found to be effective clinically for treatment of rheumatoid arthritis (RA). However, the molecular properties of CII could be changed during the preparation process. In the present study, we isolated CII from chick sternal
Toxicology, 309, 30-38 (2013-04-30)
An association between protein allergenicity and resistance to pepsin digestion in the gastrointestinal tract has been proposed. However, although widely accepted, such an association is inconsistent with known labile allergens and resistant nonallergens. Given the central role of antigen presenting
Applied and environmental microbiology, 79(6), 1843-1849 (2013-01-15)
Lactoferrin is an iron-binding glycoprotein found in the milk of most mammals for which various biological functions have been reported, such as antimicrobial activity and bifidogenic activity. In this study, we compared the bifidogenic activity of bovine lactoferrin (bLF) and
Food chemistry, 138(2-3), 923-930 (2013-02-16)
Our previous report showed that yam dioscorin and its peptic hydrolysates exhibit radical scavenging activities; however, the functions of these peptic hydrolases are still under investigation. In this study, the thiol-containing peptides derived from computer-aided simulation of pepsin hydrolysis of
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