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4370285

Sigma-Aldrich

Trypsin, TPCK-Treated

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Synonym(s):
Trypsin, TPCK treated for Cell Culture
EC Number:
NACRES:
NA.56

shipped in

dry ice

storage temp.

−20°C

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T75754352157T2601
Sigma-Aldrich

4370285

Trypsin, TPCK-Treated

Sigma-Aldrich

T7575

Trypsin Singles, Proteomics Grade

Sigma-Aldrich

4352157

Trypsin, TPCK-Treated

StableCell™ Trypsin Solution 1X, sterile-filtered, BioReagent, suitable for cell culture, 0.5 g porcine trypsin and 0.2 g EDTA, 4Na per liter of Hanks′ Balanced Salt Solution with phenol red

T2601

StableCell Trypsin Solution

shipped in

dry ice

shipped in

-

shipped in

dry ice

shipped in

wet ice

General description

Trypsin is a serine protease that specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. This modified trypsin has been treated with N-tosyl-L-phenylalanine chloromethyl ketone (TPCK) to inactivate extraneous chymotryptic activity. Each package contains 8 vials, with 25 μg in each vial.

Application

Trypsin, TPCK-Treated has been used:
  • as a supplement in Dulbecco′s Modified Eagle Medium (DMEM) for porcine delta coronavirus (PDCoV) infection experiments using epithelial-like pig kidney cell line (LLC-PK1)
  • to detach the human umbilical vein endothelial cells (HUVEC) for annexin-V/propidium Iodide (PI) staining assay
  • in minimum essential medium (MEM) for multicycle replication kinetics

Biochem/physiol Actions

N-p-Tosyl-L-phenylalanine chloromethyl ketone (TPCK) serves as an irreversible inhibitor of chymotrypsin. Trypsin induces human fibrocyte differentiation. Trypsin is widely used in proteomics for protein sample digestion. In cell culture, trypsinization is carried out to dislodge adherent cells from each other and the walls of the culture vessel.

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Customers Also Viewed

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Michael J V White et al.
PloS one, 8(8), e70795-e70795 (2013-08-21)
Trypsin-containing topical treatments can be used to speed wound healing, although the mechanism of action is unknown. To help form granulation tissue and heal wounds, monocytes leave the circulation, enter the wound tissue, and differentiate into fibroblast-like cells called fibrocytes.
Zdeněk Perutka et al.
Molecules (Basel, Switzerland), 23(10) (2018-10-17)
Trypsin is the protease of choice for protein sample digestion in proteomics. The most typical active forms are the single-chain β-trypsin and the two-chain α-trypsin, which is produced by a limited autolysis of β-trypsin. An additional intra-chain split leads to
Zhonghui Ling et al.
Reproductive biology, 21(2), 100483-100483 (2021-02-26)
Vascular endothelial cell damage is regarded as the carrier in the progression of the pathological changes of preeclampsia (PE) from the placenta to maternal organs. MicroRNA (miR)-141-3p was aberrantly expressed during PE pathogenesis. We investigated the role of miR-141-3p in
Yu Bai et al.
Microbial pathogenesis, 150, 104645-104645 (2020-12-08)
Influenza virus is responsible for significant morbidity and mortality worldwide. Acute lung injury (ALI)/acute respiratory distress syndrome (ARDS) is the major cause of death in influenza virus infected patients. Recent studies indicated that active glucagon like peptide-1 (GLP-1) encoded by
Marcel Gischke et al.
Virulence, 12(1), 666-678 (2021-02-05)
To date, only low pathogenic (LP) H5 and H7 avian influenza viruses (AIV) have been observed to naturally shift to a highly pathogenic (HP) phenotype after mutation of the monobasic hemagglutinin (HA) cleavage site (HACS) to polybasic motifs. The LPAIV

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