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Merck
모든 사진(1)

주요 문서

T8802

Sigma-Aldrich

Trypsin from bovine pancreas

TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

bovine pancreas

Quality Level

무균

aseptically filled

형태

essentially salt-free, lyophilized powder

특이 활성도

≥10,000 BAEE units/mg protein

분자량

23.8 kDa

구성

protein, ≥95%

solubility

hydrochloric acid: soluble 1 mM, clear

외래 활성

Chymotrypsin ≤0.1 BTEE units/mg protein

저장 온도

−20°C

유사한 제품을 찾으십니까? 방문 제품 비교 안내

일반 설명

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

애플리케이션

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.
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. Trypsin has also been used in a study to investigate BN-PAGE analysis of Trichoderma harzianum secretome.

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.

단위 정의

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path).
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

TPCK treated

분석 메모

Protein determined by E1%/280

기타 정보

View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer

픽토그램

Health hazardExclamation mark

신호어

Danger

유해 및 위험 성명서

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

표적 기관

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

개인 보호 장비

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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.

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Hang Lin et al.
Journal of separation science, 42(11), 1980-1989 (2019-04-05)
A novel strategy was successfully developed for screening trypsin inhibitors in traditional Chinese medicines based on monolithic capillary immobilized enzyme reactors combined with liquid chromatography-tandem mass spectrometry. Organic polymer based monolithic enzyme reactors were firstly prepared by covalently bonding trypsin
De-Lin Zhang et al.
Acta biochimica et biophysica Sinica, 44(8), 703-711 (2012-06-28)
The folding of protein, an important process for protein to fulfill normal functions, takes place in crowded physiological environments. α-Lactalbumin, as a model system for protein-folding studies, has been used extensively because it can form stable molten globule states under
John C Tran et al.
Analytical chemistry, 80(5), 1568-1573 (2008-01-31)
Although well-established as a technique for protein purification, the application of continuous elution tube gel electrophoresis to proteome fractionation remains problematic. Difficulties associated with sample collection, particularly at the high mass range or at low sample loadings, continue to plague
A E M Jørgensen et al.
Osteoarthritis and cartilage, 30(6), 886-895 (2022-04-01)
Cartilage collagen has very limited repair potential, though some turnover and incorporation has not been fully excluded. We aim to determine the regional turnover of human osteoarthritis cartilage. Patients scheduled for knee joint replacement surgery due to osteoarthritis were recruited
Adelson Joel da Silva et al.
Proteomics, 12(17), 2729-2738 (2012-06-30)
Plant cell wall-degrading enzymes produced by microorganisms possess important biotechnological applications, including biofuel production. Some anaerobic bacteria are able to produce multienzymatic complexes called cellulosomes while filamentous fungi normally secrete individual hydrolytic enzymes that act synergistically for polysaccharide degradation. Here

프로토콜

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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