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TLCK is an irreversible, specific inhibotor of the Serin-protease Trypsin and inhibits the Thrombin-like protease Cerastocytin. Together with the competitive inhibitors benzamidin hydrochlorid or 8M urea Trypsin does not show inhibitiory effects. Chymotrypsin is not inhibited by TLCK. The pH optimum for inhibition through Histidin modification is pH 7.5. Chymotrypsinogen is not inhibited by TLCK. A concentration of 50 µg/mL of TLCK inhibits 100% of the Trypsin like proteinase activity of wheat seat extracts. Besides proteases also protein kinases are inhibited by TLCK. Obviously by the modification of the enzymatic activity centre of the protein kinases. TLCK solutions are most stable at pH 6.0 at +4°C. TLCK is not stable at pH above 7.0. Therefore stock solutions of 1 mg/mL to 20 mg/mL are prepared with buffer solutions of pH below 6.0. Always pipete shortly before the inhibition experiment. Working solutionsa are: 50 µg/mL to 100 µg/mL. You will find further protease inhibitors here: Inhibitors >: Pepstatin A >, AEBSF >, Leupeptin >, TLCK >, PMSF >, Bestatine > or Diisopropylphosphorofluoridat (DFP) >.

Description:Aprotinin is mainly obtained from bovine lung. Aprotinin consists of 58 amino acids of 6511 Da and is very basic, whereby amino acids 13-18 of Aprotinin are of particular importance for binding to serine proteases. As Aprotinin has been described by various research groups, two names have become established: 1. bovine pancreatic trypsin inhibitor (BPTI) and 2. trypsin-kallikrein inhibitor (TKI). Aprotinin is often used as a non-specific serine protease inhibitor, especially for inhibition of Trypsin. Effect:Aprotinin inhibits proteases such as Trypsin, Plasmin, Chymotrypsin and Thrombin. Aprotinin is a competitive inhibitor of serine proteases that forms stable complexes with the enzyme and blocks active enzyme sites. These bindings are reversible and most aprotinin-protease complexes dissolve at very low or high pH values (<3 and >10).Application:Aprotinin is mainly used as a trypsin inhibitor. Stability: Aprotinin can be stored in lyophylised form at +2°C to +8°C for an unlimited period of time. In salt or buffer solutions (pH 5 - 8), Aprotinin is stable for at least one month at +2°C to +8°C or for several years at -20°C. Stock solutions (e.g. 10mg/mL) should be frozen in small aliquots and used only once to avoid repeated freezing and thawing. Unit definition:One trypsin inhibitory unit (TIU) inhibits the activity of 2 trypsin units by 50%, whereby one trypsin unit hydrolyses 1 μmol Nα-benzoyl-DL-arginine-p-nitroanilide (BAPNA) per minute at pH 7.8 and 25°C. 1 TIU (trypsin inhibitory unit) corresponds to approx. 1300 KIU (kallikrein inhibitory units) and 1 TIU corresponds to one Ph. Eur. unit.

TPCK is an irreversible, specific inhibotor for chymotrypsin and inhibits the thrombin-like protease Cerastocytin. Trypsin is not inhibited by TPCK. The pH optimum for inhibition throµgh alkylation by TPCK of Chymotrypsin is pH7.2. Chymotrypsinogen is not inhibited by TPCK. The bacterial Serin-proteases Re, Fa and So from E.coli are completely inhibited by 0.5 to 1 mM TPCK. TPCK is used for the production of Chymotrypsin free Trypsin. TPCK solutions are stable at pH below 7.0 at RT, nevertheless it is recommended to store solutions at +2°C to +8°C. TPCK is not stable at pH above 7.0. Stock solutions of 3mg/mL to 20mg/mL are prepared in MeOH or EtOH. Working concentrations: 10µg/mL to 100µg/mL. You will find further protease inhibitors here: Inhibitors >: Pepstatin A >, AEBSF >, Leupeptin >, TLCK >, PMSF >, Bestatine > or Diisopropylphosphorofluoridat (DFP) >.

L-Methionine sulfoximine is a potent inhibitor of glutamine sythetase activity, that is widely used as a selection agent for plasmid integration in Chinese hamster ovary (CHO) and other mammalian cell lines. The growing demand for high yield cell banks for production of recombinant proteins for therapeutics has resulted in two major systems for selection of stable and active clones, Methotrexate selection of dihydrofolate reductase (DHFR) overexpressing cells and MSX selection of glutamine synthetase overexpressing cells. Cells are grown in the absence of glutamine in the media and inhibition of the endogenous activity of glutamine synthease results in cell death for cells lacking overexpression. The MSX-glutamine synthase selection mechanism provides benefits over that of the Methotrexate-DHFR system in that it typically requires a single amplification step and results in significant reduction of time to produce high stability, highly amplified clones. Methionine sulfoximine (MSX) increases ornithine decarboxylase activity, decreases the survival rate in a model of transient cerebral ischemia, and inhibits glutamine synthetase activity. You will find further protease inhibitors here: Inhibitors >: Pepstatin A >, AEBSF >, Leupeptin >, TLCK >, PMSF >, Bestatine > or Diisopropylphosphorofluoridat (DFP) >.

Mixture of 6 protease inhibitors with a broad range activity against aspartate-, cysteine-, serine-, and metallo proteases as well as aminopeptidases. It is especially formulated for use with extracts from mammalian tissue, but can also be used with other extracts. This ready-to-use mix is free of EDTA and contains AEBSF >, Aprotinin >, E-64 >, Leupeptin >, Bestatine >, and Pepstatin A >. The kit is supplied with an extra vial of 1mL ultrapure DMSO. The content of 1 vial dissolved in 1mL DMSO will give a 100-fold concentrate, suitable for the treatment of 100mL extract. Activity spectrumAEBSF is an inhibitor against Serine proteases. Aprotinin is an inhibitor against Serine proteases. E-64 is an inhibitor against Cysteine proteases. Leupeptin is an inhibitor against Cystein proteases and trypsin-like Serine proteases. Peptstatin A is an inhibitor against Aspartic proteases. Bestatin is an inhibitor against Aminopeptidase B and Leucine-Aminopeptidases. More ready-to-use protease inhibitor mixes can be found here: - Protease-Inhibitor-Mix I > (general applications, contains no EDTA) - Protease-Inhibitor-Mix II > (general applications, contains EDTA)- Protease-Inhibitor-Mix III > (formulated for use with bacterial extracts, contains EDTA)- Protease-Inhibitor-Mix IV > formulated for use with plant extracts, contains no EDTA)- Protease-Inhibitor-Mix V > (formulated for use with mammalian extracts, contains no EDTA) You will find further protease inhibitors here: Inhibitors >: Pepstatin A >, AEBSF >, Leupeptin >, TLCK >, PMSF >, Bestatine > or Diisopropylphosphorofluoridat (DFP) >.