|Related Categories||3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Cell Dissociation,|
|form||essentially salt-free, lyophilized powder|
|mol wt||mol wt 25 kDa|
|solubility||1 mM HCl: soluble10 mg/mL, clear|
|Gene Information||cow ... CTRB1(618826)|
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Protein determined by A
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
Derived from New Zealand-sourced pancreas.
TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
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40-60 units/mg protein, vial of 5 mg
Certificate of Analysis
Certificate of Origin
|Precautionary statements||P261-P305 + P351 + P338-P342 + P311|
|Personal Protective Equipment||dust mask type N95 (US), Eyeshields, Faceshields, Gloves|
|Hazard Codes (Europe)||Xn|
|Risk Statements (Europe)||36/37/38-42|
|Safety Statements (Europe)||22-24-26-36/37|
2. SCOPE The scope of this procedure includes products that have a specification for Chymotrypsin activity. This assay procedure is not to be used to assay Chymotrypsin, Insoluble, Sigma-Aldrich Prod...
Keywords: Extinction coefficient
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Geiger, R. Methods of Enzymatic Analysis 5, 99, (1984)
Blow, D.M. Acc. Chem. Res. 9, 145, (1976)
Rick, W. Methods of Enzymatic Analysis 1, 1045, (1974)
Simulated gastrointestinal digestion of Pru ar 3 apricot allergen: assessment of allergen resistance and characterization of the peptides by ultra-performance liquid chromatography/electrospray ionisation mass spectrometry. Prandi B, Farioli L, Tedeschi T, et al. Rapid Commun. Mass Spectrom. 26(24), 2905-12, (2012)
Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC-MS. Dechavanne V, Vilbois F, Glez L, et al. Protein Expr. Purif. 87(2), 100-10, (2013)
Efficient preparation of giant vesicles as biomimetic compartment systems with high entrapment yields for biomacromolecules. Kuroiwa T, Fujita R, Kobayashi I, et al. Chem. Biodivers. 9(11), 2453-72, (2012)
Screening of whey protein isolate hydrolysates for their dual functionality: influence of heat pre-treatment and enzyme specificity. Adjonu R, Doran G, Torley P, et al. Food Chem. 136(3-4), 1435-43, (2013)
Assembly of a concentric Förster resonance energy transfer relay on a quantum dot scaffold: characterization and application to multiplexed protease sensing. Algar WR, Ancona MG, Malanoski AP, et al. ACS Nano 6(12), 11044-58, (2012)
Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance. Khan S, Rammeloo AW, and Heikkila JJ PLoS ONE 7(11), e50547, (2012)
Screening for lactic acid bacteria capable of inhibiting Campylobacter jejuni in in vitro simulations of the broiler chicken caecal environment. Robyn J, Rasschaert G, Messens W, et al. Benef. Microbes 3(4), 299-308, (2012)
The impact of ingested potato type II inhibitors on the production of the major serine proteases in the gut of Helicoverpa armigera. Stevens JA, Dunse KM, Guarino RF, et al. Insect Biochem. Mol. Biol. 43(2), 197-208, (2013)
Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native α-lactalbumin purification. Lisak K, Toro-Sierra J, Kulozik U, et al. J. Dairy Res. 80(1), 14-20, (2013)
Lung injury-dependent oxidative status and chymotrypsin-like activity of skeletal muscles in hamsters with experimental emphysema. Tonon J, Cecchini AL, Brunnquell CR, et al. BMC Musculoskelet. Disord. 14, 39, (2013)
Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation. Batra J, Szabó A, Caulfield TR, et al. J. Biol. Chem. 288(14), 9848-59, (2013)
Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum. Kellers P Acta Crystallogr. F, Struct. Biol. Cryst. Commun. 64(Pt 8), 719-22, (2008)
Robust autoactivation, chymotrypsin C independence and diminished secretion define a subset of hereditary pancreatitis-associated cationic trypsinogen mutants. Geisz A, Hegyi P, and Sahin-Tóth M FEBS J. 280(12), 2888-99, (2013)
Simplicity within the complexity: bilateral impact of DMSO on the functional and unfolding patterns of α-chymotrypsin. Tretyakova T, Shushanyan M, Partskhaladze T, et al. Biophys. Chem. 175-176, 17-27, (2013)
PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis. Zhang C, Hekmatfar S, Ramanathan A, et al. Biotechnol. Prog. 29(2), 493-504, (2013)
Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity. Roussel A, Mathieu M, Dobbs A, et al. J. Biol. Chem. 276(42), 38893-8, (2001)
Desnuelle, P. The Enzymes, (1960) 4, 93
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