T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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About This Item
Prodotti consigliati
Origine biologica
bovine pancreas (trypsin)
Livello qualitativo
Stato
buffered aqueous suspension
Concentrazione
≥15 units/mL (packed gel)
Grado di funzionalizzazione
≥15 units per mL packed gel
Matrice
cross-linked beaded agarose
Condizioni di spedizione
wet ice
Temperatura di conservazione
2-8°C
Categorie correlate
Descrizione generale
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.
Applicazioni
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.
Altre note
Insolubilized
Definizione di unità
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
Stato fisico
Suspension in approx. 10 mM acetic acid, pH 3.2
Avvertenze
Warning
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
Organi bersaglio
Respiratory system
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Dispositivi di protezione individuale
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
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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%
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
Variable activation of immune response by quinoa (Chenopodium quinoa Willd.) prolamins in celiac disease
American Journal of Clinical Nutrition, 96(2), 337-344 (2012)
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Coeliac disease (CD) is an inflammatory disorder of the small intestine. It includes aberrant adaptive immunity with presentation of CD toxic gluten peptides by HLA-DQ2 or DQ8 molecules to gluten-sensitive T cells. A ω-gliadin/C-hordein peptide (QPFPQPEQPFPW) and a rye-derived secalin
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