T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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About This Item
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
42020142
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
bovine pancreas (trypsin)
Forme
buffered aqueous suspension
Concentration
≥15 units/mL (packed gel)
Ampleur du marquage
≥15 units per mL packed gel
Matrice
cross-linked beaded agarose
Conditions d'expédition
wet ice
Température de stockage
2-8°C
Catégories apparentées
Description générale
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.
Autres remarques
Insolubilized
Définition de l'unité
One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).
Forme physique
Suspension in approx. 10 mM acetic acid, pH 3.2
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Équipement de protection individuelle
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
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Les clients ont également consulté
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
Variable activation of immune response by quinoa (Chenopodium quinoa Willd.) prolamins in celiac disease
Zevallos VF, et al.
American Journal of Clinical Nutrition, 96(2), 337-344 (2012)
Pablo Ávalos Prado et al.
iScience, 24(9), 102961-102961 (2021-08-31)
Activation and sensitization of trigeminal ganglia (TG) sensory neurons, leading to the release of pro-inflammatory peptides such as calcitonin gene-related peptide (CGRP), are likely a key component in migraine-related headache induction. Reducing TG neuron excitability represents therefore an attractive alternative
Widya A Wahab et al.
International journal of experimental pathology, 97(4), 303-309 (2016-09-24)
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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