T1763
Trypsin Agarose
buffered aqueous suspension, from bovine pancreas trypsin
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关于此项目
Biological source:
bovine pancreas (trypsin)
Concentration:
≥15 units/mL (packed gel)
产品名称
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
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
存储类别
10 - Combustible liquids
wgk
WGK 3
ppe
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
法规信息
低风险生物材料
此项目有
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)
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
John P Hobson et al.
The Journal of biological chemistry, 279(45), 46981-46994 (2004-08-26)
We report the identification and functional analysis of a type II transmembrane serine protease encoded by the mouse differentially expressed in squamous cell carcinoma (DESC) 1 gene, and the definition of a cluster of seven homologous DESC1-like genes within a
S C Bracken et al.
Alimentary pharmacology & therapeutics, 23(9), 1307-1314 (2006-04-25)
In coeliac disease, wheat, barley and rye are traditionally excluded in the gluten-free diet. However, few studies have examined the small intestinal immune response to barley and rye. To investigate the immunogenicity of barley and rye prolamins (hordein and secalin
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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