A potent inhibitor of chymotrypsin and chymase
Technical Support & Resources

Information provided in the product description is from published literature. Due to the nature of scientific experimentation, your results (e.g., selectivity and effective concentrations) or specific application for this product may differ. If you have questions about how this product fits your application, please contact our technical support staff.

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

Chymostatin

Item No. 15114

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
CAS Number
9076-44-2
Molecular Formula
C31H41O6N7
Formula Weight
607.7
Purity
≥95% (a mixture of A, B, C)
Formulation (Request formulation change)
A crystalline solid
Solubility(Learn about Variance in Solubility)
DMSO: 10 mg/mlDMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml
SMILES
N=C1NCC[C@@H]([C@H](NC(N[C@@H](CC2=CC=CC=C2)C(O)=O)=O)C(N[C@@H](CC(C)C)C(N[C@@H](CC3=CC=CC=C3)C([H])=O)=O)=O)N1.N=C4NCC[C@@H]([C@H](NC(N[C@@H](CC5=CC=CC=C5)C(O)=O)=O)C(N[C@@H](C(CC)C)C(N[C@@H](CC6=CC=CC=C6)C([H])=O)=O)=O)N4.N=C7NCC[C@@H]([C@H](NC(N[C@@H](CC8=CC=CC=C8)C(O)=O)=O)C(N[C@@H](C(C)C)C(N[C@@H](CC9=CC=CC=C9)C([H])=O)=O)=O)N7
InChi Code
InChI=1S/2C31H41N7O6.C30H39N7O6/c1-19(2)15-24(27(40)34-22(18-39)16-20-9-5-3-6-10-20)35-28(41)26(23-13-14-33-30(32)36-23)38-31(44)37-25(29(42)43)17-21-11-7-4-8-12-21;1-3-19(2)25(27(40)34-22(18-39)16-20-10-6-4-7-11-20)37-28(41)26(23-14-15-33-30(32)35-23)38-31(44)36-24(29(42)43)17-21-12-8-5-9-13-21;1-18(2)24(26(39)33-21(17-38)15-19-9-5-3-6-10-19)36-27(40)25(22-13-14-32-29(31)34-22)37-30(43)35-23(28(41)42)16-20-11-7-4-8-12-20/h3-12,18-19,22-26H,13-17H2,1-2H3,(H,34,40)(H,35,41)(H,42,43)(H3,32,33,36)(H2,37,38,44);4-13,18-19,22-26H,3,14-17H2,1-2H3,(H,34,40)(H,37,41)(H,42,43)(H3,32,33,35)(H2,36,38,44);3-12,17-18,21-25H,13-16H2,1-2H3,(H,33,39)(H,36,40)(H,41,42)(H3,31,32,34)(H2,35,37,43)/t22-,23-,24?,25-,26-;19?,22-,23-,24-,25?,26-;21-,22-,23-,24?,25-/m000/s1
InChi Key
QJIJPLFVFWXMGK-XUICXHRPSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

Download most recent Certificate of Analysis for this product

    5 mg

    $112

    Add

    10 mg

    $209

    Add

    25 mg

    $468

    Add

    50 mg

    $876

    Add
    Product Description

    Chymostatin is a bioactive peptide of microbial origin that acts as a protease inhibitor with selectivity for chymotryptase-like serine proteases.1 It potently inhibits chymotrypsin and chymase (Ki = 9.36 and 13.1 nM, respectively) while less effectively blocking the activity of cathepsins, papain, and leukocyte elastase.2,1,3,4,5 It is without effect on trypsin, thrombin, plasmin, pepsin, and kallikrein.1

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Umezawa, H., Aoyagi, T., Morishima, H., et al. Chymostatin, a new chymotrypsin inhibitor produced by actinomycetes. J. Antibiot. (Tokyo) 23(8), 425-427 (1970).

    2. Akahoshi, F., Ashimori, A., Sakashita, H., et al. Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase. J. Med. Chem. 44(8), 1297-1304 (2001).

    3. Feinstein, G., Malemud, C.J., and Janoff, A. The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin. Biochim. Biophys. Acta 429(3), 925-932 (1976).

    4. Stein, R.L., and Strimpler, A.M. Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin. Biochemistry 26(9), 2611-2615 (1987).

    5. Yamamoto, K., Takeda, M., and Kato, Y. Characteristics of activation of cathepsin B by sodium salicylate and comparison of catalytic site properties of cathepsins B and H. Jpn. J. Pharmacol. 39(2), 207-215 (1985).