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α-Chymotrypsin (CAS 9004-07-3)

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Alternate Names:
TLCK-Chymotrypsin
Application:
α-Chymotrypsin is A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains on the carboxyl end of the bond
CAS Number:
9004-07-3
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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α-Chymotrypsin is an essential digestive enzyme responsible for the degradation of proteins within the digestive system. As a serine protease enzyme, it exhibits the ability to cleave proteins at specific amino acids, namely arginine, lysine, and tyrosine, by targeting their carboxyl side. Originating from the pancreas, α-chymotrypsin is released into the small intestine to facilitate the breakdown of proteins into smaller peptides and individual amino acids. Moreover, α-chymotrypsin finds utility in laboratory investigations centered on exploring the structure and functionality of proteins.


α-Chymotrypsin (CAS 9004-07-3) References

  1. Alpha-chymotrypsin catalysis in imidazolium-based ionic liquids.  |  Laszlo, JA. and Compton, DL. 2001. Biotechnol Bioeng. 75: 181-6. PMID: 11536140
  2. Effects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin.  |  Simon, LM., et al. 2002. Biochem Biophys Res Commun. 293: 416-20. PMID: 12054616
  3. Ultrafast surface hydration dynamics and expression of protein functionality: alpha -Chymotrypsin.  |  Pal, SK., et al. 2002. Proc Natl Acad Sci U S A. 99: 15297-302. PMID: 12427971
  4. Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.  |  Pallarès, I., et al. 2004. J Mol Biol. 342: 321-31. PMID: 15313627
  5. Tunable inhibition and denaturation of alpha-chymotrypsin with amino acid-functionalized gold nanoparticles.  |  You, CC., et al. 2005. J Am Chem Soc. 127: 12873-81. PMID: 16159281
  6. Modulation of the catalytic behavior of alpha-chymotrypsin at monolayer-protected nanoparticle surfaces.  |  You, CC., et al. 2006. J Am Chem Soc. 128: 14612-8. PMID: 17090046
  7. Product inhibition of alpha-chymotrypsin in reverse micelles.  |  Bru, R. and Walde, P. 1991. Eur J Biochem. 199: 95-103. PMID: 1712303
  8. Reversible photoregulation of binding of alpha-chymotrypsin to a gold surface.  |  Pearson, D., et al. 2007. J Am Chem Soc. 129: 14862-3. PMID: 17994751
  9. Osmolyte counteracts urea-induced denaturation of alpha-chymotrypsin.  |  Venkatesu, P., et al. 2009. J Phys Chem B. 113: 5327-38. PMID: 19354310
  10. Overview of the stability of α-chymotrypsin in different solvent media.  |  Kumar, A. and Venkatesu, P. 2012. Chem Rev. 112: 4283-307. PMID: 22506806
  11. Molecular aspects of the interaction of spermidine and α-chymotrypsin.  |  Farhadian, S., et al. 2016. Int J Biol Macromol. 92: 523-532. PMID: 27456119
  12. Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.  |  Fujinaga, M., et al. 1987. J Mol Biol. 195: 397-418. PMID: 3477645
  13. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin.  |  Greene, RF. and Pace, CN. 1974. J Biol Chem. 249: 5388-93. PMID: 4416801
  14. Synthesis and characterization of a bioluminogenic substrate for alpha-chymotrypsin.  |  Monsees, T., et al. 1994. Anal Biochem. 221: 329-34. PMID: 7810874

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

α-Chymotrypsin, 1 g

sc-473609
1 g
$219.00