T4424
Trypsin solution from porcine pancreas
1 ×, sterile-filtered, BioReagent, suitable for cell culture, 2.5 g porcine trypsin per liter in Hanks′ Balanced Salt Solution with phenol red
생물학적 소스
Porcine pancreas
Quality Level
무균
sterile-filtered
제품 라인
BioReagent
양식
solution
분자량
23.4 kDa
농도
1 ×
기술
cell culture | mammalian: suitable
불순물
Porcine parvovirus, none detected (9 CFR)
pH
7.0-7.6
배송 상태
dry ice
저장 온도
−20°C
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애플리케이션
Trypsin solution from porcine pancreas has been used for keratinocyte isolation and staining. It has also been used as a component of CMF-Steinberg′s solution to replace heart tissues after centrifugation in a study to culture embryonic cardiomyocytes from Mexican axolotl.
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.
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.
생화학적/생리학적 작용
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.
주의사항
This product should be stored frozen at -20°C
단위 정의
One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
제조 메모
This is a 2.5 g/L porcine trypsin solution in Hank′s Balanced Salt Solution with phenol red.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
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