4370285
Trypsin, TPCK-Treated
Synonyme(s) :
Trypsin, TPCK treated for Cell Culture
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About This Item
Produits recommandés
Conditions d'expédition
dry ice
Température de stockage
−20°C
Catégories apparentées
Description générale
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
Actions biochimiques/physiologiques
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.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
10 - Combustible liquids
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
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
Jian-Ping Dai et al.
International journal of molecular sciences, 19(4) (2018-03-24)
Oxymatrine (OMT) is a strong immunosuppressive agent that has been used in the clinic for many years. In the present study, by using plaque inhibition, luciferase reporter plasmids, qRT-PCR, western blotting, and ELISA assays, we have investigated the effect and
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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