- Trypsin inhibitor
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- $0.00 / 1g
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2026-02-13
- CAS:9035-81-8
- Min. Order: 1g
- Purity: BR,4000BAEEu/mg
- Supply Ability: 1kg/month
- Trypsin inhibitor
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- $1.00 / 1KG
-
2019-07-12
- CAS:9035-81-8
- Min. Order: 1KG
- Purity: 99%
- Supply Ability: 25kg
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| | Trypsin inhibitor Basic information |
| | Trypsin inhibitor Chemical Properties |
| storage temp. | -20°C | | solubility | H2O: >10 mg/mL | | form | solution | | color | White to off-white | | PH | <7.4 | | biological source | Phaseolus limensis (lima bean) | | Water Solubility | Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). | | Specific Activity | ≥7,000units/mg protein |
| Hazard Codes | Xn | | Risk Statements | 42/43 | | Safety Statements | 22-36/37-45-23 | | WGK Germany | 3 | | F | 10-21 | | HS Code | 35040090 | | Storage Class | 11 - Combustible Solids | | Hazard Classifications | Resp. Sens. 1
Skin Sens. 1 |
| | Trypsin inhibitor Usage And Synthesis |
| Chemical Properties | It is a kinin release enzyme inhibitor extracted from bovine pancreas, lungs, gills and other tissues. It is not an enzyme itself, and is an alkaline polypeptide consisting of 58 amino acid residues, with the whole molecule in pear shape, and lysine as the active center. It can compete with the activity center of many proteases for a lysyl group and inhibit their activities. It is white or slightly yellow powder, odorless, soluble in water, dialyzable, with isoelectric point of 10-10.5. It is stable to high temperature, acid, alkali and enzyme. It is stable to high temperature, acid, alkali and enzyme. It can be heated to 100℃ in dilute acid, and it is still stable when placed at room temperature for 24h at pH12.6, but its vitality starts to decrease at pH12.8. In 60-80 ℃ can be thermophilic protease digestion, other enzymes can not inactivate it. | | Uses | This product has been tested for cell culture applications. Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a ton-toxigenic mangrove isolate of Vibri sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin. | | Uses | Trypsin Inhibitor, Corn is a specific reversible inhibitor of trypsin and potent inhibitor of human factor XIIa. | | Uses | Trypsin inhibitor from chicken egg white has been used:
- to produce denatured, oxidized and deglycosylated ovomucoid and used to stimulate patient derived cell cultures for mapping T cell epitopes
- to treat nuclei for flow cytometric analysis
- in Holtfreter′s solution, used for the dissociation of planarians into cells
| | General Description | Ovomucoid or trypsin inhibitor is an abundant protein in most avian egg whites. The hen′s egg protein is composed of about 186 amino acid residues, and is highly glycosylated. Three tandem domains are each homologous with pancreatic trypsin inhibitor. It is highly immunogenic, and probably accounts for most cases of egg allergy. | | Biochem/physiol Actions | This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent. |
| | Trypsin inhibitor Preparation Products And Raw materials |
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