- Chymotrypsin
-
- $0.00 / 1kg
-
2024-04-22
- CAS:9004-07-3
- Min. Order: 1kg
- Purity: 99.8%
- Supply Ability: 1000 kg
- Chymotrypsin
-
- $10.00 / 1ASSAYS
-
2021-12-10
- CAS:9004-07-3
- Min. Order: 1ASSAYS
- Purity: 99.9%
- Supply Ability: 8000kgs/month
- Chymotrypsin
-
- $78.00 / 1KG
-
2021-10-20
- CAS:9004-07-3
- Min. Order: 1KG
- Purity: 99%
- Supply Ability: 9000kg/per week
|
| | Chymotrypsin Basic information |
| | Chymotrypsin Chemical Properties |
| Melting point | 127°C | | density | 1.37[at 20℃] | | vapor pressure | 0Pa at 25℃ | | storage temp. | -20°C | | solubility | Reconstitute in 1mM HCl. Soluble at 10mg/ml in 1mM HCl. 2mM calcium chloride serves as a stabilizer. Store aliquoted solutions at -20°C for up to a week. | | form | salt-free, lyophilized powder | | color | white | | Water Solubility | 125g/L at 25℃ | | Merck | 13,2282 | | LogP | -1.3 at 20℃ | | EPA Substance Registry System | Chymotrypsin (9004-07-3) |
| | Chymotrypsin Usage And Synthesis |
| Chemical Properties | Lyophilized powder, dialyzed | | Uses | The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration. | | Uses | α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin. | | Uses | α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers. | | General Description | Chymotrypsin (Chymar) is extractedfrom mammalian pancreas and is used in cataractsurgery. A dilute solution is used to irrigate the posteriorchamber of the eye to dissolve the fine filaments that holdthe lens. | | Biochem/physiol Actions | α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, α2-macroglobulin, 10 mM Cu2+ and Hg2+. | | Purification Methods | α-Chymotrypsin is crystallised twice from four-tenths saturated ammonium sulfate solution, then dissolved in 1mM HCl and dialysed against 1mM HCl at 2-4o. The solution is stored at 2o [Lang et al. J Am Chem Soc 80 4923 1958]. |
| | Chymotrypsin Preparation Products And Raw materials |
|