Product Details
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9002-07-7 Name |
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Name |
Trypsin |
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Synonym |
Trypsin-EDTA Solution 1X;α-and β-trypsin;Tryprar;Trypsevas;Trypsin Powder, Porcine 1:250;TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS;TRYPSIN, PROTEOMICS SEQUENCING GRADE;TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES |
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9002-07-7 Chemical & Physical Properties |
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Melting point |
115°C |
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Density |
1.37[at 20℃] |
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Molecular Formula |
C6H15O12P3 |
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Molecular Weight |
372.1 |
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Appearance of Characters |
lyophilized powder |
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Storage condition |
−20°C |
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Stability |
Stable. Incompatible with strong oxidizing agents. |
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Water Solubility |
Reconstitute in aqueous buffer | Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). |
Trypsin is an enzyme that has been extensively studied in scholarly articles for its various applications in medicine. One of its primary uses is in the field of wound healing and tissue regeneration. Trypsin has been found to possess potent proteolytic activity, which makes it effective in debriding and removing necrotic tissue from wounds. It aids in the removal of dead tissue, promoting the formation of granulation tissue and accelerating the healing process. Additionally, trypsin has been investigated for its potential applications in the treatment of conditions such as chronic ulcers, burns, and surgical wounds. It can be used as a topical agent or incorporated into wound dressings to enhance the debridement and healing process. Furthermore, trypsin has been studied for its potential applications in cell culture and tissue engineering, where it is used to dissociate cells and facilitate cell isolation and expansion.
A crystalline protein compound has been isolated from a solution containing crystalline trypsin and crystalline soybean inhibitor. The protein consists of about equal weights of trypsin and of the inhibitor.
Original articles resulting from studies in animal models, in bacterial culture, and using cells that describe antibacterial action of trypsin inhibitor-type peptides or proteins were selected in PubMed, Science Direct, Scopus, Web of Science, BVS, and EMBASE. The methodological quality assessment was performed using the PRISMA and OHAT tool. 2382 articles were retrieved, 17 of which were eligible.
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