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1494057

USP

Pancreatin amylase and protease

United States Pharmacopeia (USP) Reference Standard

Sinónimos:

Pancreatin

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About This Item

Número de CAS:
UNSPSC Code:
41116107
NACRES:
NA.24

grade

pharmaceutical primary standard

manufacturer/tradename

USP

application(s)

pharmaceutical (small molecule)

format

neat

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General description

Pancreatin amylase and protease USP Reference Standard is provided as delivered and specified by the issuing Pharmacopoeia. All information provided in support of this product, including SDS and any product information leaflets have been developed and issued under the Authority of the issuing Pharmacopoeia. For further information and support please go to the website of the issuing Pharmacopoeia.

Application


  • Pancreatin for digestive enzyme research: Pancreatin, a mixture of digestive enzymes including amylase and protease, is extensively used in biochemical studies to understand digestive processes. It is pivotal in research focusing on enzyme mechanisms in the gastrointestinal tract and their role in nutrient absorption and digestion (Saruc et al., 2012).

  • High-activity pancreatin for protein digestion studies: The potent activity of pancreatin′s proteolytic and amylolytic enzymes is utilized in scientific studies to dissect the pathways of protein and starch breakdown. This research is fundamental for developing improved therapeutic agents and understanding metabolic diseases linked to protein and carbohydrate metabolism (Gonçalvez et al., 1998).

  • Pharmaceutical applications: In the pharmaceutical industry, pancreatin′s enzymes are applied in the formulation of medications that require precise digestive enzymes to activate or enhance drug delivery mechanisms, particularly in treatments targeting the digestive system (Friess et al., 1998).

Unit Definition

One USP Unit of amylase activity is contained in the amount of pancreatin that decomposes starch at an initial rate such that 0.16 µEq of glycosidic linkage is hydrolyzed per minute under the conditions of the Assay for amylase activity. One USP Unit of protease activity is contained in the amount of pancreatin that under the conditions of the Assay for protease activity hydrolyzes casein at an initial rate such that there is liberated per minute an amount of peptides not precipitated by trichloroacetic acid that gives the same absorbance at 280 nm as 15 nmol of tyrosine.

Analysis Note

These products are for test and assay use only. They are not meant for administration to humans or animals and cannot be used to diagnose, treat, or cure diseases of any kind.  ​

Other Notes

This product is part of the USP Biologics program.
Sales restrictions may apply.

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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B N P Sah et al.
Journal of dairy science, 99(6), 4233-4242 (2016-03-21)
The search for alternative therapeutics is on the rise due to the extensive increase in bacterial resistance to various conventional antibiotics and side effects of conventional cancer therapies. Bioactive peptides released from natural sources such as dairy foods by lactic
Pancrelipase
United States Pharmacopeia and National Formulary
United States Pharmacopeia, 3382-3382 (2013)
Pancreatin
United States Pharmacopeia and National Formulary
United States Pharmacopeia, 3379-3379 (2013)
Yangchao Luo et al.
Food chemistry, 155, 146-154 (2014-03-07)
Sodium caseinate (NaCas) was hydrolyzed by papain, pancreatin and trypsin from 10 min to 24h, and the hydrolysates were partially characterized for several important properties. At the studied conditions, papain and trypsin were more effective in hydrolyzing NaCas than pancreatin.

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