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T8802
Trypsin from bovine pancreas
TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein
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About This Item
Polecane produkty
pochodzenie biologiczne
bovine pancreas
Poziom jakości
sterylność
aseptically filled
Formularz
essentially salt-free, lyophilized powder
aktywność właściwa
≥10,000 BAEE units/mg protein
masa cząsteczkowa
23.8 kDa
skład
protein, ≥95%
rozpuszczalność
hydrochloric acid: soluble 1 mM, clear
obecność zanieczyszczeń
Chymotrypsin ≤0.1 BTEE units/mg protein
temp. przechowywania
−20°C
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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.
Zastosowanie
For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. Trypsin has also been used in a study to investigate BN-PAGE analysis of Trichoderma harzianum secretome.
Działania biochem./fizjol.
Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Definicja jednostki
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path).
One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
Uwaga dotycząca przygotowania
TPCK treated
Komentarz do analizy
Protein determined by E1%/280
Inne uwagi
View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer
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Inhibitor
Numer produktu
Opis
Cennik
substrat
Numer produktu
Opis
Cennik
Hasło ostrzegawcze
Danger
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organy docelowe
Respiratory system
Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 1
Środki ochrony indywidualnej
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Protokoły
This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).
Ciągła spektrofotometryczna metoda oznaczania szybkości przy użyciu substratu BAEE mierzy aktywność trypsyny, niezbędną do charakterystyki enzymu.
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