| Description | DescriptionClostripain also known as Clostridiopeptidase B or Endoproteinase Arg-C is a proteinase that cleaves peptide bonds on the carboxyl side of arginine. This protein is a heterodimer composed of a heavy and a light chain that are held together via strong noncovalent forces. As a proteolytic DescriptionClostripain also known as Clostridiopeptidase B or Endoproteinase Arg-C is a proteinase that cleaves peptide bonds on the carboxyl side of arginine. This protein is a heterodimer composed of a heavy and a light chain that are held together via strong noncovalent forces. As a proteolytic enzyme it can be used for isolation of various cell types by tissue dissociation.Clostripain exists in two different forms, an oxidized, native condition and a reduced activated form that differ in enzymatic activity. The native clostripain can be activated with reducing agents (e.g. DTT, Cysteine) resulting in a higher activity of the enzyme.ApplicationClostripain NB is used in combination with Collagenase NB 1 and/or Neutral Protease NB, suitable for cell isolation from various tissue types.SpecificationsContains chromatographically highly purified clostripain.Clostripain, native state activity: ≥ 5.0 U/mg (BAEE)Clostripain, activated activity: ≥ 50.0 U/mg (BAEE)Clostripain activity, native state, per vial: ≥ 200 U/vial (BAEE)Clostripain activity, activated, per vial: statusEC 3.4.24.3 • Mr ca. 59 000 • CAS [9028-00-6]References and DefinitionsUnit definition:Clostripain, native state (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8.Clostripain, activated (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8. The enzyme is activated with 2.5 mM DTT. References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Kula et al. (1976) Biochem. Biophys. Res. Commun. 69, 389-396... Read More | Unit Definition One unit will cause a change in A600 of 0.330 per minute at pH 5.7 at 37°C in a 2.0 ml reaction mixture (45 minute assay) | IRE1α kinase-IN-2 is a potent IRE1α kinase inhibitor, with an EC 50 of 0.82 µM. IRE1α kinase-IN-2 inhibits IRE1α kinase autophosphorylation (IC 50 =3.12 µM). IRE1α kinase-IN-2 inhibits XBP1 mRNA splicing in the WT cell lines.In VitroIRE1α kinase-IN-2 (compoundIRE1α kinase-IN-2 is a potent IRE1α kinase inhibitor, with an EC 50 of 0.82 µM. IRE1α kinase-IN-2 inhibits IRE1α kinase autophosphorylation (IC 50 =3.12 µM). IRE1α kinase-IN-2 inhibits XBP1 mRNA splicing in the WT cell lines.In VitroIRE1α kinase-IN-2 (compound 3) inhibits XBP1 mRNA splicing, even during ER stress. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... Read More |