The present invention relates to activators of caspase-8/c-FLIP.sub.L dimerization and their use in enhancing the pro-apoptotic activity of the heterodimer and cancer therapy.

The present invention relates to activators of caspase-8/c-FLIP.sub.L dimerization and their use in enhancing the pro-apoptotic activity of the heterodimer and cancer therapy.

An object of the present invention is to provide a method for measuring tryptase activity in a blood sample accurately and rapidly by a convenient operation in order to accurately evaluate the state of a disease whose state involves mast cells. The present invention enables tryptase activity in a blood sample to be directly measured without the pretreatment, such as purification or concentration, of the blood sample, using a substrate for measuring tryptase activity, comprising a tripeptide C-terminally linked through a peptide bond to a dye label, selected from the following formulas (1) to (3): (1) Lys-Ala-Arg-X, (2) Ala-Ala-Arg-X, and (3) Abu-Ala-Arg-X (wherein X represents a dye label whose fluorescence characteristics or color development characteristics change upon the cleavage of the peptide bond with Arg, and Abu represents 2-aminobutyric acid).

An object of the present invention is to provide a method for measuring tryptase activity in a blood sample accurately and rapidly by a convenient operation in order to accurately evaluate the state of a disease whose state involves mast cells. The present invention enables tryptase activity in a blood sample to be directly measured without the pretreatment, such as purification or concentration, of the blood sample, using a substrate for measuring tryptase activity, comprising a tripeptide C-terminally linked through a peptide bond to a dye label, selected from the following formulas (1) to (3): (1) Lys-Ala-Arg-X, (2) Ala-Ala-Arg-X, and (3) Abu-Ala-Arg-X (wherein X represents a dye label whose fluorescence characteristics or color development characteristics change upon the cleavage of the peptide bond with Arg, and Abu represents 2-aminobutyric acid).

Compositions, methods, and kits are provided for assaying calpain-5 activity and inhibition. In particular, novel peptide substrates are provided for detecting calpain-5, measuring calpain-5 activity, and screening for inhibitors of calpain-5 to identify potential therapeutic agents for treating retinal diseases and other diseases associated with calpain-5 hyperactivity. Additionally, novel inhibitors of calpain-5 are also provided.

Compositions, methods, and kits are provided for assaying calpain-5 activity and inhibition. In particular, novel peptide substrates are provided for detecting calpain-5, measuring calpain-5 activity, and screening for inhibitors of calpain-5 to identify potential therapeutic agents for treating retinal diseases and other diseases associated with calpain-5 hyperactivity. Additionally, novel inhibitors of calpain-5 are also provided.

The present invention relates to the technical field of chemical analysis and quantitative detection, in particular to a quantitative detection method for snake venom thrombin-like enzyme (SVTLE) from Agkistrodon halys pallas. The quantitative detection method for the SVTLE includes the following steps of taking a reference substance of marker peptide for the SVTLE from Agkistrodon halys pallas with an amino acid sequence of LDSPVSNSAHIAPLSLPSSAPSVGSVCR, and preparing a series of reference solutions with different concentrations; adding the reference solutions in test solutions respectively for enzymolysis, and then taking a supernatant after enzymolysis as a series of solutions to be detected; and adding the solutions to be detected in a liquid chromatogram-mass spectrometer, and then selecting a qualitative ion pair and a quantitative ion pair to detect contents of marker peptide in the solutions to be detected.

The present invention relates to the technical field of chemical analysis and quantitative detection, in particular to a quantitative detection method for snake venom thrombin-like enzyme (SVTLE) from Agkistrodon halys pallas. The quantitative detection method for the SVTLE includes the following steps of taking a reference substance of marker peptide for the SVTLE from Agkistrodon halys pallas with an amino acid sequence of LDSPVSNSAHIAPLSLPSSAPSVGSVCR, and preparing a series of reference solutions with different concentrations; adding the reference solutions in test solutions respectively for enzymolysis, and then taking a supernatant after enzymolysis as a series of solutions to be detected; and adding the solutions to be detected in a liquid chromatogram-mass spectrometer, and then selecting a qualitative ion pair and a quantitative ion pair to detect contents of marker peptide in the solutions to be detected.

Provided is a technology related to a horseshoe crab factor B variant, and also provided is means for performing endotoxin measurement with high sensitivity. A polypeptide having an amino acid sequence in which the amino acid residue at the 193-position in an amino acid sequence of a polypeptide of horseshoe crab factor B is substituted with a cysteine (Cys) residue, is produced. Endotoxin measurement can be carried out with high sensitivity by configuring a Limulus reagent by combining this polypeptide with horseshoe crab factor C.

Provided is a technology related to a horseshoe crab factor B variant, and also provided is means for performing endotoxin measurement with high sensitivity. A polypeptide having an amino acid sequence in which the amino acid residue at the 193-position in an amino acid sequence of a polypeptide of horseshoe crab factor B is substituted with a cysteine (Cys) residue, is produced. Endotoxin measurement can be carried out with high sensitivity by configuring a Limulus reagent by combining this polypeptide with horseshoe crab factor C.