T1005
Trypsin from bovine pancreas
Type XI, lyophilized powder, ≥6,000 BAEE units/mg protein
Szinonimák:
Serine Protease 1
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(5)
About This Item
Javasolt termékek
biológiai forrás
bovine pancreas
Minőségi szint
típus
Type XI
form
lyophilized powder
specifikus aktivitás
≥6,000 BAEE units/mg protein
molekulatömeg
23.8 kDa
összetétel
protein, 90-100%
szennyeződések
salt, essentially free
oldhatóság
hydrochloric acid: soluble 1 mM, clear
idegen aktivitás
Chymotrypsin ≤0.1 BTEE units/mg protein
tárolási hőmérséklet
−20°C
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Alkalmazás
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 from bovine pancreas has been used:-
- For Trypsinization, for eliminating the membrane bound alloantigen.
- For incubating 20-kD amylase-binding component, to evaluate its Chemical nature.
- To prepare lactoferrin degradation products for evaluating its antiadipogenic activity.
Biokémiai/fiziológiai hatások
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.
Komponensek
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.
Vigyázat
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.
Egység definíció
One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
Elkészítési megjegyzés
This product is from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL.
inhibitor
Product No.
Leírás
Árazás
szubsztrát
Product No.
Leírás
Árazás
Figyelmeztetés
Danger
Figyelmeztető mondatok
Óvintézkedésre vonatkozó mondatok
Veszélyességi osztályok
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Célzott szervek
Respiratory system
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 1
Egyéni védőeszköz
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Protocols
Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.
Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.
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