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T1763

Sigma-Aldrich

Trypsin Agarose

buffered aqueous suspension, from bovine pancreas trypsin

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
42020142
NACRES:
NA.54

biological source

bovine pancreas (trypsin)

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

Signal Word

Warning

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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
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
Raquel Olías et al.
Food research international (Ottawa, Ont.), 169, 112825-112825 (2023-05-31)
The presence of so-called anti-nutritional factors can reduce the bioavailability of nutrients following consumption of seeds which are otherwise an excellent source of proteins, carbohydrates and micronutrients. Among the proteins associated with negative effects on quality in pea (Pisum sativum
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
S J Fisher et al.
Acta crystallographica. Section D, Biological crystallography, 68(Pt 7), 800-809 (2012-07-04)
A bond-distance analysis has been undertaken to determine the protonation states of ionizable amino acids in trypsin, subtilisin and lysozyme. The diffraction resolutions were 1.2 Å for trypsin (97% complete, 12% H-atom visibility at 2.5σ), 1.26 Å for subtilisin (100% complete, 11%

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