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관련 카테고리
일반 설명
Trypsin is a major proteolytic enzyme, synthesized as a preproenzyme by pancreas and is stored as proenzyme trypsinogen in secretory granules. Trypsin belongs to the family of serine proteases that are characterized by the catalytic triad His57, Asp102 and Ser195. Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0. This product is prepared from recombinant trypsin, porcine sequence. It is naturally devoid of chymotryptic activity. This high-quality trypsin is suitable for proteomics use.
생화학적/생리학적 작용
Trypsin plays an important role in the digestion of consumed protein and contributes to the activation of other proteolytic enzymes like chemotrypsin and elastase.
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3
표적 기관
Respiratory system
보충제 위험성
Storage Class Code
8A - Combustible corrosive hazardous materials
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus)
European Food Research and Technology, 232(3), 381-388 (2011)
Autophagy receptor NDP52 alters DNA conformation to modulate RNA polymerase II transcription.
Nature Communications, 14, 2855-2855 (2023)
Molecular characterization and gene expression of six trypsinogens in the flatfish Senegalese sole (Solea senegalensis Kaup) during larval development and in tissues
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 149(2), 334-344 (2008)
Handbook of Proteolytic Enzymes (2012)
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