Phe-Pro-Arg-PABA-Resorufin is a Chromogenic and fluorogenic peptide substrate for the highly sensitive detection of proteases in biological matrices. The substrate is also applicable to the sensitive detection of the thrombin inhibitor dabigatran in human
Bz-IEGR-pNA is a colorimetric substrate for Factor Xa.1 Factor Xa preferentially binds to and cleaves the Ile-Glu-Gly-Arg (IEGR) peptide sequence to release p-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of Factor Xa activity.References1. Aruell, L., Friberger, P., Karlsson, G., et al. A new sensitive and highly specific chromogenic peptide substrate for factor Xa. Thromb. Res. 11(5), 595-609 (1977). Bz-IEGR-pNA is a colorimetric substrate for Factor Xa.1 Factor Xa preferentially binds to and cleaves the Ile-Glu-Gly-Arg (IEGR) peptide sequence to release p-nitroanilide (pNA), which can be quantified by colorimetric detection at 405 nm as a measure of Factor Xa activity. References1. Aruell, L., Friberger, P., Karlsson, G., et al. A new sensitive and highly specific chromogenic peptide substrate for factor Xa. Thromb. Res. 11(5), 595-609 (1977).
Diheptanoyl Thio-PC is a substrate for all phospholipase A2s (PLA2s) with the exception of cPLA2 and PAF-acetyl hydrolase (PAF-AH). Interaction of this compound with a PLA2 results in cleavage of the sn-2 fatty acid generating a free thiol on the lysophospholipid. This free thiol can be detected using chromogenic substrates such as DTNB (Ellman's reagent) and DTP.
Thioester analogs of glycerophospholipids, in combination with Ellman's reagent, are convenient colorimetric substrates for the measurement of phospholipase (PL) activity. Palmitoyl thio-PC is a chromogenic PLA2 substrate that contains a palmitoyl thioester at the sn-2 position of the glycerol backbone. Hydrolysis of the thioester by PLA2 yields a free thiol that reacts readily with DTNB (Ellman's reagent) giving a bright yellow product with an absorbance maximum at 412 nm. Palmitoyl thio-PC has been used to measure bee venom sPLA2 activity in a phospholipid:Triton X-100 mixed micelle system.
p-Nitrophenylphosphorylcholine is a chromogenic substrate that is used to measure phospholipase C (PLC) activity. Hydrolysis of p-nitrophenylphosphorylcholine by PLC results in the liberation of p-nitrophenol, which can be measured at 405 nm at pH 7.2-7.5.
4-Nitrophenyl β-D-cellotrioside is a chromogenic substrate for endoglucanases and cellobiohydrolases. Hydrolysis of this substrate by these enzymes liberates 4-nitrophenol, which generates a yellow color that is measured by monitoring absorbance at 405 nm.
N-acetyl-D-galactosaminidase catalyzes the cleavage of N-acetylglucosamine (GlcNAc), the monomeric unit of the polymer chitin. 4-Nitrophenyl-N-acetyl-α-D-galactosaminide can be used as a chromogenic substrate for N-acetyl-D-galactosaminidase, generating a yellow solution upon cleavage.