T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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About This Item
UNSPSC Code:
12352204
eCl@ss:
42020142
NACRES:
NA.54
MDL number:
Biological source:
bovine pancreas (trypsin)
Concentration:
≥15 units/mL (packed gel)
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
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General description
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.
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.
Application
Trypsin Agarose has been used for enzymatic hydrolysis of prolamins and gliadin to generate peptides.
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.
Physical form
Suspension in approx. 10 mM acetic acid, pH 3.2
Other Notes
Insolubilized
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
Storage Class
10 - Combustible liquids
wgk
WGK 3
ppe
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
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G Bolte et al.
Clinica chimica acta; international journal of clinical chemistry, 247(1-2), 59-70 (1996-03-29)
For many years, peptic-tryptic digests of gliadin, known as Frazer's fraction III, have been used in investigations of gliadin effects. Potential contamination by the proteases pepsin and trypsin, however, was not considered. To investigate the influence of contaminating proteases on
Coeliac disease: immunogenicity studies of barley hordein and rye secalin-derived peptides
Wahab WA, et al.
International Journal of Experimental Pathology, 97(4), 303-309 (2016)
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
Bovine trypsin immobilization on agarose activated with divinylsulfone: Improved activity and stability via multipoint covalent attachment
Dos s, et al.
Journal of Molecular Catalysis. B, Enzymatic, 117(4), 38-44 (2015)
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
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