Merck
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T4799

Sigma-Aldrich

Trypsin from porcine pancreas

lyophilized powder, BioReagent, suitable for cell culture, 1,000-2,000 BAEE units/mg solid

Sinónimos:
Cocoonase, Tryptase, Tryptar
Número de CAS:
Comisión internacional de enzimas:
Número de EC:
Número MDL:
NACRES:
NA.75

origen biológico

Porcine pancreas

Nivel de calidad

200

línea de producto

BioReagent

formulario

lyophilized powder

specific activity

1,000-2,000 BAEE units/mg solid

mol peso

23.8 kDa

concentración

25 mg/mL

technique(s)

cell culture | mammalian: suitable

pH

7.6

enviado en

ambient

temp. de almacenamiento

−20°C

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Descripción general

Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization.

Aplicación

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 digestionsns†. 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 from porcine pancreas has been used to digest chicken bones. It has also been used in the isolation of luteal endothelial cells.

Envase

5, 10, 25, 100, 500 g in poly bottle

Acciones bioquímicas o fisiológicas

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.

Componentes

Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.

Precaución

Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS.

Definición de unidad

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25° C using BAEE as substrate. One BTEE unit = 320 ATEE units. Reaction volume = 3.2 mL (1 cm light path).

Nota de preparación

This product is a lyophilized powder soluble in Hank′s Balanced Salt Solution at 25 mg/mL.
For applications that require EDTA, solubilizing trypsin should be done with a buffered salt solution contaiing no Ca2+ or Mg2+.

pictogramas

Exclamation markHealth hazard

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

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

Órganos de actuación

Respiratory system

Código de clase de almacenamiento

11 - Combustible Solids

WGK

WGK 1

Equipo de protección personal

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

Certificado de Análisis

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Certificado de origen

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Effects of storage and passage of bovine luteal endothelial cells on endothelin-1 and prostaglandin F2alpha production
Acosta TJ, et al.
Journal of Reproduction and Development, 53(3), 473-480 (2007)
Prostaglandin F2alpha regulates the nitric oxide generating system in bovine luteal endothelial cells
Lee SH, et al.
Journal of Reproduction and Development, 55(4), 418-424 (2009)
The development of angiotensin I-converting enzyme inhibitor derived from chicken bone protein
Animal Science Journal = Nihon Chikusan Gakkaiho, 79(1), 122-128 (2008)
Effects of tea polyphenols on the activities of ?-amylase, pepsin, trypsin and lipase (2007)
Effects of tumor necrosis factor alpha and Interferon gamma on the viability and mRNA expression of TNF receptor type I in endothelial cells from the bovine corpus luteum
Hojo T, et al.
Journal of Reproduction and Development, 56(5), 515-519 (2010)

Protocolos

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

Contenido relacionado

Trypsin Serine Protease Enzyme

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

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