T8658
Trypsin from bovine pancreas
suitable for protein sequencing, lyophilized powder
Synonim(y):
Porcine Trypsin, Trypsin for Mass Spectropetry
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About This Item
Polecane produkty
klasa czystości
Proteomics Grade
Postać
lyophilized powder
masa cząsteczkowa
23.8 kDa
opakowanie
vial of 100 μg
rozpuszczalność
hydrochloric acid: soluble 1 mM, clear
przydatność
suitable for protein sequencing
temp. przechowywania
−20°C
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Zastosowanie
- Trypsin from bovine pancreas has been used for in-gel digestion for MS (mass spectrometry) analysis.
- It has been used for the digestion of albumin for size-exclusion chromatography.
- It has been used for the digestion of HDL (high density lipoprotein) for LC-MS (liquid chromatography-mass spectrometry) analysis.
- It has been used for limited proteolysis of IST1 (putative MAPK-activating protein PM28).
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.
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.
Komponenty
Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.
Przestroga
Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.
Definicja jednostki
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
This product is from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL.
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
Certyfikaty analizy (CoA)
Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.
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