Trypsin from porcine pancreas

CAS Number:	9002-07-7
Enzyme Commission (EC) Number:	3.4.21.4 ( BRENDA | IUBMB )
EC Number:	232-650-8
MDL number:	MFCD00082094
NACRES:	NA.75

Кат. номер

T4799-PM

T4799-2KG

T4799-100G

T4799-10G

T4799-5G

T4799-25G

T4799-2KG-KC

T4799-500G

T4799-10X5G

Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization.
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 digestionsns†. 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 porcine pancreas has been used to digest chicken bones. It has also been used in the isolation of luteal endothelial cells.
5, 10, 25, 100, 500 g in poly bottle
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.
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.
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.
One BAEE unit will produce a A253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. One BTEE unit = 320 ATEE units. Reaction volume = 3.2 mL (1 cm light path).
This product is a lyophilized powder soluble in Hanks Balanced Salt Solution at 25 mg/mL.
For applications that require EDTA, solubilizing trypsin should be done with a buffered salt solution contaiing no Ca2+ or Mg2+.

biological source	Porcine pancreas
Quality Level	200
product line	BioReagent
form	lyophilized powder
specific activity	1,000-2,000 BAEE units/mg solid
mol wt	23.8 kDa
concentration	25 mg/mL
application(s)	cell culture | mammalian: suitable
pH	7.6
shipped in	ambient
storage temp.	−20°C

Pictograms	GHS07,GHS08
Signal Word	Danger
Hazard Statements	H315 - H319 - H334 - H335
Precautionary Statements	P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338
Target Organs	Respiratory system
Personal Protective Equipment	dust mask type N95 (US), Eyeshields, Faceshields, Gloves
RIDADR	NONH for all modes of transport
WGK Germany	WGK 1