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Inhibitor of trypsin and trypsin-like proteases
BML-PI121-0200 200 mg 134.00 USD
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Irreversible inhibitor of trypsin and trypsin-like serine proteases such as granzyme D and tryptase. Also inhibits other proteases including plasmin, thrombin, and papain and some kinases including PKC. Inhibits LPS-induced expression of COX-2 in macrophages. Inhibits apoptosis (possibly through the inhibition of serine proteases). Chymotrypsin is not inhibited by TLCK, so this inhibitor can be used to block contaminating trypsin activity in chymoptrypsin preparations. TLCK can be used in combination with a chymotrypsin inhibitor to prevent proteolytic degradation during the isolation of proteins.

Product Details

Alternative Name:Nα-Tosyl-Lys-chloromethylketone . HCl
Formula:C14H21CIN2O3S . HCl
Purity:≥95% (HPLC)
Appearance:Off-white solid
Solubility:Soluble in methanol (50mg/ml), DMSO (5mM) or water. Stock solutions at concentrations up to 10mM can be prepared in aqueous buffers with a pH of 6.0 or lower. TLCK is very unstable in buffers with a pH higher than 6 and will decompose rapidly.
Shipping:Blue Ice
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only
BML-PI121 structure
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BML-PI121 structure

Product Literature References

The small heat shock protein B8 (HSPB8) confers resistance to bortezomib by promoting autophagic removal of misfolded proteins in multiple myeloma cells: M. Hamouda, et al.; Oncotarget 5, 6252 (2014), Application(s): Analysis of velcade resistant multiple myeloma human cells by WB, Assay, Abstract; Full Text
A novel form of the RelA nuclear factor kappaB subunit is induced by and forms a complex with the proto-oncogene c-Myc: N.R. Chapman, et al.; Biochem. J. 366, 459 (2002), Abstract;
Lipopolysaccharide-induced expression of cyclooxygenase-2 in mouse macrophages is inhibited by chloromethylketones and a direct inhibitor of NF-kappa B translocation: A. Abate, et al.; Prostaglandins Other Lipid Mediat. 56, 277 (1998), Abstract;
15N and 1H NMR spectroscopy of the catalytic histidine in chloromethyl ketone-inhibited complexes of serine proteases: E. Tsilikounas, et al.; Biochemistry 35, 2437 (1996), Abstract;
DNA degradation and proteolysis in thymocyte apoptosis: H.O. Fearnhead, et al.; Toxicol. Lett. 82/83, 135 (1995), Abstract;
Granzymes, a family of serine proteases released from granules of cytolytic T lymphocytes upon T cell receptor stimulation: D.E. Jenne, et al.; Immunol. Rev. 103, 53 (1988), Abstract;
Tryptase in rat mast cells: properties and inhibition by various inhibitors in comparison with chymase: M. Muramatu, et al.; Biol. Chem. Hoppe Seyler 369, 617 (1988), Abstract;
N-alpha-Tosyl-L-lysine chloromethyl ketone and N-alpha-tosyl-L-phenylalanine chloromethyl ketone inhibit protein kinase C: D.H. Solomon; FEBS Lett. 190, 342 (1985), Abstract;
Isolation and characterization of the histone variants in chicken erythrocytes: M.K. Urban, et al.; Biochemistry 18, 3952 (1979), Abstract;
Inhibition of human thrombin assessed with different substrates and inhibitors. Characterization of fibrinopeptide binding interaction: J.J. Gorman; Biochim. Biophys. Acta. 412, 273 (1975), Abstract;
Kinetics of inhibition of papain by TLCK and TPCK in the presence of BAEE as substrate: B.C. Wothers; FEBS Lett. 2, 143 (1969), Abstract;
Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from N-tosyl-L-lysine: E. Shaw, et al.; Biochemistry 4, 2219 (1965),

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