Cas no 9001-12-1 (Collagenase from Clostridium histolyticum(Animal Origin Free,A))

Collagenase from Clostridium histolyticum (Animal Origin Free, A) is a highly purified enzyme preparation designed for applications requiring the digestion of collagen and other extracellular matrix components. This product is derived from a bacterial source, ensuring freedom from animal-derived materials, which minimizes the risk of viral or prion contamination. It exhibits high specific activity and consistent performance, making it suitable for tissue dissociation, cell isolation, and research in regenerative medicine. The enzyme is rigorously tested for purity and functionality, ensuring reliable results in sensitive experimental workflows. Its animal-origin-free formulation aligns with regulatory requirements for therapeutic and diagnostic applications.
Collagenase from Clostridium histolyticum(Animal Origin Free,A) structure
9001-12-1 structure
Product Name:Collagenase from Clostridium histolyticum(Animal Origin Free,A)
CAS No:9001-12-1
MF:C60H100N2
MW:849.4
MDL:MFCD00130830
CID:48124
PubChem ID:44384985
Update Time:2025-06-14

Collagenase from Clostridium histolyticum(Animal Origin Free,A) Chemical and Physical Properties

Names and Identifiers

    • Collagenase
    • COLLAGENASE TYPE X
    • Collagenase from Clostridium histolyticum
    • collagenase crude type ia cell culture*tested
    • collagenase F. clostridium histolyticum
    • collagenase from achromobacter iophagus
    • collagenase sterile filtered type vii-S
    • collagenase type I-S
    • collagenase type vii
    • CollagenaseⅠ
    • CollagenaseⅤ
    • CollagenaseⅢ
    • CollagenaseⅣ
    • CollagenaseⅡ
    • Collagenase from Clostridium histolyticum(Purified)
    • Collagenase from Clostridium histolyticum(Type 2)
    • Aspergillopeptidase C
    • Azocollase
    • Clostridiopeptidase A
    • Clostridiopeptidase I
    • Clostridiopeptidase II
    • Clostridium histolyticum collagenase
    • Collagen peptidase
    • Collagen protease
    • Collagenase A
    • Matrix metalloprotease-1
    • Metallocollagenase
    • Santyl
    • Soycollagestin
    • (5S,6S,9R,10S,13S,17S,23S,24S,27R,28S,31S,35S)-5,6,9,13,17,23,24,27,31,35-Decamethyl-10,28-dioctyl-2
    • Collagenase I
    • Collagenase Type II
    • CID 44384985
    • Collagenase D
    • Collagenase type 1
    • Collagenase type A
    • Collagenase type I
    • Collagenolytic enzymes
    • Collalatine
    • Collalitine
    • Endoenzymes, collagenolytic
    • Enzymes, collagen-degrading
    • Euphaulysin
    • Matrix metalloprotease MMP-ABT
    • Morikraz
    • Nucleolysin
    • Preprocollagenase
    • Collagenase from Clostridium histolyticum(Animal Origin Free,B)
    • 9001-12-1
    • CHEMBL176323
    • (5S,6S,9R,10S,13S,17S,23S,24S,27R,28S,31S,35S)-5,6,9,13,17,23,24,27,31,35-Decamethyl-10,28-dioctyl-2,20-diazanonacyclo[19.15.0.03,19.05,17.06,14.09,13.023,35.024,32.027,31]hexatriaconta-1(21),2,19-triene
    • YRQNKMKHABXEJZ-UVQQGXFZSA-N
    • Collagenase from Clostridium histolyticum(Animal Origin Free,A)
    • MDL: MFCD00130830
    • Inchi: 1S/C60H100N2/c1-13-15-17-19-21-23-25-43-27-33-55(7)49-29-31-51(3)39-45-47(41-59(51,11)57(49,9)37-35-53(43,55)5)61-46-40-52(4)32-30-50-56(8)34-28-44(26-24-22-20-18-16-14-2)54(56,6)36-38-58(50,10)60(52,12)42-48(46)62-45/h43-44,49-50H,13-42H2,1-12H3/t43-,44-,49?,50?,51-,52-,53+,54+,55-,56-,57-,58-,59-,60-/m0/s1
    • InChI Key: YRQNKMKHABXEJZ-UVQQGXFZSA-N
    • SMILES: N1C2=C(C([H])([H])[C@@]3(C([H])([H])[H])[C@](C([H])([H])[H])(C2([H])[H])C([H])([H])C([H])([H])C2([H])[C@]4(C([H])([H])[H])C([H])([H])C([H])([H])[C@]([H])(C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H])[C@@]4(C([H])([H])[H])C([H])([H])C([H])([H])[C@@]23C([H])([H])[H])N=C2C=1C([H])([H])[C@@]1(C([H])([H])[H])[C@](C([H])([H])[H])(C2([H])[H])C([H])([H])C([H])([H])C2([H])[C@]3(C([H])([H])[H])C([H])([H])C([H])([H])[C@]([H])(C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H])[C@@]3(C([H])([H])[H])C([H])([H])C([H])([H])[C@@]21C([H])([H])[H]

Computed Properties

  • Exact Mass: 848.78865120g/mol
  • Monoisotopic Mass: 848.78865120g/mol
  • Isotope Atom Count: 0
  • Hydrogen Bond Donor Count: 0
  • Hydrogen Bond Acceptor Count: 2
  • Heavy Atom Count: 62
  • Rotatable Bond Count: 14
  • Complexity: 1490
  • Covalently-Bonded Unit Count: 1
  • Defined Atom Stereocenter Count: 12
  • Undefined Atom Stereocenter Count : 2
  • Defined Bond Stereocenter Count: 0
  • Undefined Bond Stereocenter Count: 0
  • XLogP3: 21.9
  • Topological Polar Surface Area: 25.8

Experimental Properties

  • Color/Form: Light brown odorless low freezing powder
  • Melting Point: No data available
  • Boiling Point: No data available
  • Flash Point: No data available
  • PH: 7.0
  • Solubility: Soluble in aqueous buffers.
  • Merck: 2481
  • Solubility: dissolve in water
  • Vapor Pressure: No data available

Collagenase from Clostridium histolyticum(Animal Origin Free,A) Security Information

Collagenase from Clostridium histolyticum(Animal Origin Free,A) Customs Data

  • HS CODE:3507907000

Collagenase from Clostridium histolyticum(Animal Origin Free,A) Pricemore >>

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Collagenase from Clostridium histolyticum(Animal Origin Free,A) Suppliers

Tiancheng Chemical (Jiangsu) Co., Ltd
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(CAS:9001-12-1)Collagenase
Order Number:LE9658;LE528
Stock Status:in Stock
Quantity:25KG,200KG,1000KG
Purity:99%
Pricing Information Last Updated:Friday, 20 June 2025 12:01
Price ($):discuss personally
Suzhou Senfeida Chemical Co., Ltd
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(CAS:9001-12-1)Collagenase
Order Number:sfd4369
Stock Status:in Stock
Quantity:200kg
Purity:99.9%
Pricing Information Last Updated:Friday, 19 July 2024 14:33
Price ($):discuss personally
Shanghai Joy Biotech Ltd
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(CAS:9001-12-1)Collagenase A
Order Number:JY199
Stock Status:in Stock
Quantity:100g; 1kg; 10kg; 25kg
Purity:98%
Pricing Information Last Updated:Friday, 30 May 2025 09:02
Price ($):discuss personally

Additional information on Collagenase from Clostridium histolyticum(Animal Origin Free,A)

Recent Advances in Collagenase from Clostridium histolyticum (Animal Origin Free, A) and Its Applications in Biomedicine

The enzyme Collagenase from Clostridium histolyticum (Animal Origin Free, A), with the CAS number 9001-12-1, has garnered significant attention in the field of biomedicine due to its unique ability to degrade collagen, a major structural protein in connective tissues. Recent studies have explored its applications in tissue engineering, wound healing, and therapeutic interventions for fibrotic diseases. This research brief synthesizes the latest findings on this enzyme, highlighting its mechanisms, efficacy, and potential clinical benefits.

One of the most notable advancements is the development of animal-origin-free (AOF) formulations of collagenase, which address concerns related to immunogenicity and contamination risks associated with traditional animal-derived enzymes. AOF collagenase, such as the product specified, has been shown to exhibit comparable enzymatic activity while offering enhanced safety profiles. Recent in vitro and in vivo studies have demonstrated its effectiveness in dissociating tissues for cell isolation, a critical step in regenerative medicine and cancer research.

In the context of therapeutic applications, collagenase from Clostridium histolyticum has been investigated for its role in treating Dupuytren's contracture and Peyronie's disease. Clinical trials have reported significant improvements in patients following collagenase injections, with reduced contracture and minimal adverse effects. Moreover, researchers are exploring its potential in addressing fibrotic disorders such as liver cirrhosis and pulmonary fibrosis, where excessive collagen deposition is a hallmark.

Recent methodological innovations have also optimized the production and purification of collagenase, ensuring higher yields and purity levels. Advanced techniques such as recombinant DNA technology and high-performance liquid chromatography (HPLC) have been employed to achieve these goals. These improvements are critical for scaling up production to meet the growing demand in both research and clinical settings.

Despite these advancements, challenges remain, including the need for standardized protocols to assess collagenase activity and the exploration of synergistic combinations with other enzymes or therapeutic agents. Future research directions may focus on personalized medicine approaches, where collagenase formulations are tailored to individual patient needs based on genetic or metabolic profiles.

In conclusion, Collagenase from Clostridium histolyticum (Animal Origin Free, A) represents a versatile and promising tool in biomedicine. Its applications span from basic research to clinical therapeutics, driven by ongoing innovations in production and application methodologies. Continued research and development are expected to further expand its utility and efficacy, solidifying its role in modern medical practice.

Recommended suppliers
Tiancheng Chemical (Jiangsu) Co., Ltd
(CAS:9001-12-1)Collagenase
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Purity:99%/99%
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Price ($):Inquiry/Inquiry
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Suzhou Senfeida Chemical Co., Ltd
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