This product is essentially salt-free and does not contain EDTA. Trypsin preparations that do include EDTA are typically in solution form and clearly labeled as containing this chelator.
T9935
Trypsin from bovine pancreas
essentially salt-free, lyophilized powder, ≥9,000 BAEE units/mg protein, BioReagent, suitable for cell culture
Synonym(s):
Serine Protease 1
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| Size/SKU | Availability | Price |
|---|---|---|
50 mg | Available to ship TODAYfromMILWAUKEE | $61.30 |
100 mg | Available to ship TODAYfromMILWAUKEE | $102.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-650-8
MDL number:
Specific activity:
≥9,000 BAEE units/mg protein
$61.30
Available to ship TODAYDetails
product line
BioReagent
Quality Segment
form
essentially salt-free, lyophilized powder
specific activity
≥9,000 BAEE units/mg protein
mol wt
23.8 kDa
composition
protein, ≥80%
technique(s)
cell culture | mammalian: suitable
solubility
hydrochloric acid: soluble 1 mM
storage temp.
−20°C
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 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 enzymatic digestion of nucleus pulposus (NP) cells during human NP cells isolation. It has also been used as a immunopanning reagent for purification of 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 from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL.
For applications that involve EDTA, solubilizing trypsin should be done with a buffered salt solution containing no Ca2+ or Mg2+.
For applications that involve EDTA, solubilizing trypsin should be done with a buffered salt solution containing no Ca2+ or Mg2+.
Other Notes
One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
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.
1 of 1
This Item | |||
|---|---|---|---|
| description essentially salt-free, lyophilized powder, ≥9,000 BAEE units/mg protein, BioReagent, suitable for cell culture | description Type XI, lyophilized powder, ≥6,000 BAEE units/mg protein | description TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein | description TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein |
| technique(s) cell culture | mammalian: suitable | technique(s) - | technique(s) - | technique(s) - |
| specific activity ≥9,000 BAEE units/mg protein | specific activity ≥6,000 BAEE units/mg protein | specific activity ≥10,000 BAEE units/mg protein | specific activity ≥10,000 BAEE units/mg protein |
| form essentially salt-free, lyophilized powder | form lyophilized powder | form essentially salt-free, lyophilized powder | form essentially salt-free, lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 23.8 kDa | mol wt 23.8 kDa | mol wt 23.8 kDa | mol wt 23.8 kDa |
| solubility hydrochloric acid: soluble 1 mM | solubility hydrochloric acid: soluble 1 mM, clear | solubility hydrochloric acid: soluble 1 mM | solubility hydrochloric acid: soluble 1 mM, clear |
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Danger
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Hazard Classifications
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target_organs
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Storage Class
11 - Combustible Solids
wgk
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