T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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About This Item
Numer MDL:
Kod UNSPSC:
12352204
eCl@ss:
42020142
NACRES:
NA.54
Polecane produkty
pochodzenie biologiczne
bovine pancreas (trypsin)
Postać
buffered aqueous suspension
stężenie
≥15 units/mL (packed gel)
zakres etykietowania
≥15 units per mL packed gel
macierz
cross-linked beaded agarose
Warunki transportu
wet ice
temp. przechowywania
2-8°C
Opis ogólny
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.
Zastosowanie
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.
Inne uwagi
Insolubilized
Definicja jednostki
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
Postać fizyczna
Suspension in approx. 10 mM acetic acid, pH 3.2
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Hasło ostrzegawcze
Warning
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
Organy docelowe
Respiratory system
Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 3
Środki ochrony indywidualnej
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
Certyfikaty analizy (CoA)
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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)
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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
Vanessa A Gutzeit et al.
Cell chemical biology, 28(11), 1648-1663 (2021-03-19)
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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%
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