T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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UNSPSC Code:
12352204
eCl@ss:
42020142
NACRES:
NA.54
MDL number:
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Permítanos ayudarleNombre del producto
Trypsin Agarose, buffered aqueous suspension, from bovine pancreas trypsin
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
Quality Level
Categorías relacionadas
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.
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.
Other Notes
Insolubilized
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
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 3
ppe
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
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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%
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
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