Quantitave purity testing is not performed on this product. While there may be residual salts and trace components present following the purification process, no specific excipients have been added. This material has not been TCPK-treated.
T4799
Trypsin from porcine pancreas
lyophilized powder, BioReagent, suitable for cell culture, 1,000-2,000 BAEE units/mg solid
Trypsin from porcine pancreas
Synonym(s):
Cocoonase, Tryptar, Tryptase
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| Size/SKU | Availability | Price |
|---|---|---|
5 g | Check Cart for Availability | $54.20 |
10 g | Check Cart for Availability | $99.80 |
25 g | Check Cart for Availability | $175.00 |
10 x 5 g | Check Cart for Availability | $443.00 |
100 g | Check Cart for Availability | $470.00 |
500 g | Check Cart for Availability | $2,120.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.75
EC Number:
232-650-8
MDL number:
Specific activity:
1,000-2,000 BAEE units/mg solid
Biological source:
Porcine pancreas
Concentration:
25 mg/mL
biological source
Porcine pancreas
Quality Segment
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
technique(s)
cell culture | mammalian: suitable, single cell analysis: suitable
pH
7.6
shipped in
ambient
storage temp.
−20°C
General description
Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization.
Application
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.
Biochem/physiol Actions
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.
Preparation Note
This product is a lyophilized powder soluble in Hank′s 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+.
For applications that require EDTA, solubilizing trypsin should be done with a buffered salt solution contaiing no Ca2+ or Mg2+.
Other Notes
One BAEE unit will produce a ΔA253 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).
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.
Disclaimer
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.
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This Item | |||
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable, single cell analysis: suitable | technique(s) - | technique(s) - | technique(s) - |
| biological source Porcine pancreas | biological source bovine pancreas | biological source human pancreas | biological source - |
| specific activity 1,000-2,000 BAEE units/mg solid | specific activity ≥10,000 BAEE units/mg protein | specific activity - | specific activity 13,000-20,000 BAEE units/mg protein |
| form lyophilized powder | form essentially salt-free, lyophilized powder | form salt-free, lyophilized powder | form lyophilized powder |
| concentration 25 mg/mL | concentration - | concentration - | concentration - |
| shipped in ambient | shipped in - | shipped in - | shipped in - |
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signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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