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Merck

T1763

Sigma-Aldrich

Trypsin Agarose

buffered aqueous suspension, from bovine pancreas trypsin

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About This Item

Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
42020142
NACRES:
NA.54

biological source

bovine pancreas (trypsin)

Quality Level

form

buffered aqueous suspension

concentration

≥15 units/mL (packed gel)

extent of labeling

≥15 units per mL packed gel

matrix

cross-linked beaded agarose

shipped in

wet ice

storage temp.

2-8°C

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 Agarose is an insoluble enzyme product. It is produced by reacting a conventional "soluble" enzyme (trypsin) with an inert base (agarose). This insoluble conjugate retains the activity of the original enzyme. Trypsin bound to agarose are highly stable and maintain denaturing conditions for longer time than the soluble trypsin.

Application

A very active and very stable trypsin agarose derivative has been used to optimize the design of the synthesis of a model dipeptide, benzoylarginine leucinamide. Trypsin has also been used in a study to investigate protonation-state determination in proteins using high-resolution X-ray crystallography.
Trypsin Agarose has been used for enzymatic hydrolysis of prolamins and gliadin to generate peptides.

Other Notes

Insolubilized

Unit Definition

One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).

Physical form

Suspension in approx. 10 mM acetic acid, pH 3.2

pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


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Amit Tripathi et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(39), 16799-16804 (2009-10-07)
Increased intestinal permeability (IP) has emerged recently as a common underlying mechanism in the pathogenesis of allergic, inflammatory, and autoimmune diseases. The characterization of zonulin, the only physiological mediator known to regulate IP reversibly, has remained elusive. Through proteomic analysis
R M Blanco et al.
Enzyme and microbial technology, 13(7), 573-583 (1991-07-01)
By using very active and very stable trypsin agarose derivatives, we have optimized the design of the synthesis of a model dipeptide, benzoylarginine leucinamide, by two different strategies: (i) kinetically controlled synthesis (KCS), by using benzoyl arginine ethyl ester and
S C Bracken et al.
Alimentary pharmacology & therapeutics, 23(9), 1307-1314 (2006-04-25)
In coeliac disease, wheat, barley and rye are traditionally excluded in the gluten-free diet. However, few studies have examined the small intestinal immune response to barley and rye. To investigate the immunogenicity of barley and rye prolamins (hordein and secalin
Jie Jiang et al.
Nature chemistry, 15(4), 578-586 (2023-02-23)
The discovery of crosstalk effects on the renin-angiotensin system (RAS) is limited by the lack of approaches to quantitatively monitor, in real time, multiple components with subtle differences and short half-lives. Here we report a nanopore framework to quantitatively determine
Vanessa A Gutzeit et al.
Cell chemical biology, 28(11), 1648-1663 (2021-03-19)
Despite the power of photopharmacology for interrogating signaling proteins, many photopharmacological systems are limited by their efficiency, speed, or spectral properties. Here, we screen a library of azobenzene photoswitches and identify a urea-substituted "azobenzene-400" core that offers bistable switching between

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