T1005

Trypsin from bovine pancreas

Name: Trypsin from bovine pancreas
Brand: SIGMA

Type XI, lyophilized powder, ≥6,000 BAEE units/mg protein

Szinonimák:

Serine Protease 1

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez

About This Item

CAS Number:

9002-07-7

EC-szám:

3.4.21.4 (BRENDA, IUBMB)

EC-szám:

232-650-8

MDL-szám:

MFCD00082094

UNSPSC kód:

12352204

NACRES:

NA.78

Fontos dokumentumok

Összes dokumentáció megtekintése

Műszaki ügyfélszolgálat

Segítségre van szüksége? Szakértő tudósaink csapata készséggel áll az Ön rendelkezésére.

Segíthetünk?

Műszaki ügyfélszolgálat

Segítségre van szüksége? Szakértő tudósaink csapata készséggel áll az Ön rendelkezésére.

Segíthetünk?

biológiai forrás

bovine pancreas

Minőségi szint

200

típus

Type XI

Forma

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

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.

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.