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329225-25-4

C14H13ClN2OS is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 329225-25-4 Structure

  • Basic information

    1. Product Name: C14H13ClN2OS
    2. Synonyms: C14H13ClN2OS
    3. CAS NO:329225-25-4
    4. Molecular Formula:
    5. Molecular Weight: 292.789
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 329225-25-4.mol

  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: C14H13ClN2OS(CAS DataBase Reference)
    10. NIST Chemistry Reference: C14H13ClN2OS(329225-25-4)
    11. EPA Substance Registry System: C14H13ClN2OS(329225-25-4)

  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 329225-25-4(Hazardous Substances Data)

329225-25-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 329225-25-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 3,2,9,2,2 and 5 respectively; the second part has 2 digits, 2 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 329225-25:
(8*3)+(7*2)+(6*9)+(5*2)+(4*2)+(3*5)+(2*2)+(1*5)=134
134 % 10 = 4
So 329225-25-4 is a valid CAS Registry Number.

329225-25-4Downstream Products

329225-25-4Relevant articles and documents

Identification of novel, exosite-binding matrix metalloproteinase-13 inhibitor scaffolds

Roth, Joshua,Minond, Dmitriy,Darout, Etzer,Liu, Qin,Lauer, Janelle,Hodder, Peter,Fields, Gregg B.,Roush, William R.

, p. 7180 - 7184 (2012/01/15)

Matrix metalloproteinase-13 (MMP-13) has been implicated as the protease responsible for collagen degradation in cartilage during osteoarthritis (OA). Compounds that inhibit the metalloproteinase at the Zn binding site typically lack specificity among MMP family members. Analogs of the low-micromolar lead MMP-13 inhibitor 4, discovered through high-throughput screening, were synthesized to investigate structure-activity relationships in this inhibitor series. Systematic modifications of 4 led to the discovery of MMP-13 inhibitors 20 and 24 which are more selective than 4 against other MMPs. Compound 20 is also approximately fivefold more potent as an MMP-13 inhibitor than the original HTS-derived lead compound 4.

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