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T6424

Sigma-Aldrich

Trypsin from human pancreas

salt-free, lyophilized powder, vial of ≥1,000 BAEE units

Synonym(s):

Serine Protease 1

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About This Item

CAS Number:
9002-07-7
Enzyme Commission number:
3.4.21.4 (BRENDA, IUBMB)
EC Number:
232-650-8
MDL number:
MFCD01323069
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

human pancreas

Quality Level

200

form

salt-free, lyophilized powder

packaging

vial of ≥1,000 BAEE units

UniProt accession no.

P07477
P07478
P35030

storage temp.

−20°C

Gene Information

human ... PRSS1(5644) , PRSS2(5645) , PRSS3(5646)

General description

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Trypsin is a serine protease. The pancreas produce the precursor trypsinogen and secretes it to the intestine. Trypsinogen is converted to trypsin by enterokinase in the intestinal mucous membrane.

Application

Trypsin has been used in a study to assess the similarities between the hepatitis E virus and human astrovirus. Trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells.

Unit Definition

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).

Quantity

Minimum 1,000 BAEE units/vial

Analysis Note

Protein determined by E1%/280.

Other Notes

View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer

inhibitor

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Description
Pricing

B6506

Benzamidine hydrochloride hydrate, ≥99%

T9003

Trypsin inhibitor from Glycine max (soybean), lyophilized powder

M6159

α2-Macroglobulin from human plasma, BioUltra, ≥98% (SDS-PAGE)

D7910

3,4-Dichloroisocoumarin, serine protease inhibitor

D0879

Diisopropylfluorophosphate

L2023

Leupeptin trifluoroacetate salt, ≥90% (HPLC), microbial

A6191

Antipain dihydrochloride from microbial source, protease inhibitor

T9777

Trypsin-chymotrypsin inhibitor from Glycine max (soybean), lyophilized powder

A1153

Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid

P7626

Phenylmethanesulfonyl fluoride, ≥98.5% (GC)

A9024

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A6150

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

T2011

Trypsin inhibitor from chicken egg white, Type III-O (free of ovoinhibitor)

substrate

Product No.
Description
Pricing

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Industrial Enzymes and Their Applications (1998)
Kelly A Dryden et al.
Journal of molecular biology, 422(5), 650-658 (2012-06-30)
Human astroviruses (HAstVs) are a major cause of gastroenteritis. HAstV assembles from the structural protein VP90 and undergoes a cascade of proteolytic cleavages. Cleavage to VP70 is required for release of immature particles from cells, and subsequent cleavage by trypsin
Jia Liu et al.
Nature protocols, 16(7), 3522-3546 (2021-06-06)
Cellular heterogeneity is pervasive and of paramount importance in biology. Single-cell analysis techniques are indispensable for understanding the heterogeneity and functions of cells. Low-copy-number proteins (fewer than 1,000 molecules per cell) perform multiple crucial functions such as gene expression, cellular
Cynthia Luz Marcelo et al.
BMC dermatology, 12, 8-8 (2012-06-26)
Primary keratinocytes derived from epidermis, oral mucosa, and urothelium are used in construction of cell based wound healing devices and in regenerative medicine. This study presents in vitro technology that rapidly expands keratinocytes in culture by growing monolayers under large
Olivier Rivoire
Physical review letters, 110(17), 178102-178102 (2013-05-18)
Studies of coevolution of amino acids within and between proteins have revealed two types of coevolving units: coevolving contacts, which are pairs of amino acids distant along the sequence but in contact in the three-dimensional structure, and sectors, which are
View All Related Papers

Protocols

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

Related Content

Trypsin Serine Protease Enzyme

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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