| Size | Price | Stock | Qty |
|---|---|---|---|
| 100mg |
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| 250mg |
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| 500mg |
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| 1g |
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| Targets |
Microbially derived matrix metalloproteinases (MMPs) and zinc peptidase
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| ln Vitro |
Collagenase is considered important for cell migration and collagen remodeling in tissue repair and regeneration processes. Activated collagenase produces characteristic 3/4 collagen fragments
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| References | |
| Additional Infomation |
In recent years, non-invasive treatments have been widely used in the medical field. Enzymes exhibit high activity at extremely low concentrations in both laboratory and pharmaceutical applications, making them crucial in various biological phenomena related to organisms, especially in human medicine. The medical community has increasingly focused on non-invasive treatments in recent years. Researchers are dedicated to developing drugs and tools that can reduce invasive medical procedures. Collagenases are proteins that catalyze chemical reactions and break peptide bonds in collagen. Collagen production may exceed the required amount, occur at inappropriate sites, or fail to degrade after a certain period. In such cases, injecting collagenases or their ointments may aid in collagen degradation. In vitro and in vivo studies have demonstrated the efficacy of collagenases in wound healing, burns, nipple pain, and the treatment of various diseases, including herniated discs, keloids, cellulitis, and lipomas. This review describes the therapeutic applications of collagenases in the medical field and the process for producing collagenases using novel methods, paving the way for more effective and safer applications of collagenases. [1]
In recent years, the medical community has paid increasing attention to treatment methods based on non-invasive approaches. Researchers are dedicated to developing drugs and tools that can reduce invasive procedures in medical practice. Enzymes are highly selective and can exert high specificity even at very low concentrations, thus playing an important role in drug development. True collagenases can cleave the helical regions of fibrous collagen molecules under various physiological pH and temperature conditions. However, the non-helical regions of gelatin and collagen molecules are known to be degraded by a variety of mammalian proteases, including pepsin, trypsin, chymotrypsin, papain, and other tissue enzymes. Research on collagenases began at the end of the last century, followed by the isolation of an extracellular enzyme—Clostridium—and the identification and characterization of many other bacterial and mammalian collagenases. Until recently, it was believed that bacteria produced true collagenases only from a few species of bacteria, such as Clostridium and some other microorganisms, particularly a strain of Vibrio alginolyticus (formerly Achromobacter iophagus). Unlike animal collagenases (which break down the natural triple-helix structure of collagen), bacterial collagenases differ from vertebrate collagenases, which exhibit broader substrate specificity. In terms of their recently proposed applications, collagenases appear to be a convenient and inexpensive drug with the potential for treating burns, promoting wound healing, and other diseases in the near future. However, due to insufficient data and the need for further research, collagenases are not currently produced or used clinically as drugs. This review utilizes all published literature related to the therapeutic applications of collagenases in human diseases. Focusing on human diseases and collagenases, this review emphasizes the role of collagenases in treating specific diseases characterized by excessive collagen deposition. Furthermore, collagenases can be used to isolate intact animal hepatocytes, adipocytes, and adrenal cells for subsequent cell culture. In summary, this review describes the therapeutic applications of collagenases in the medical field and the processes for producing collagenases using novel methods, paving the way for more effective and safer applications. It is hoped that future research will develop methods and processes for producing collagenase from new sources, such as green bottle flies, which are non-pathogenic and crucial for wound healing. [1] |
| CAS # |
9001-12-1
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|---|---|
| Appearance |
Off-white to light brown solid
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| LogP |
21.9
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| SMILES |
CCCCCCCC[C@H]1CC[C@@]2([C@@]1(CC[C@]3(C2CC[C@@]4([C@@]3(CC5=C(C4)N=C6C[C@]7([C@@](CCC8[C@@]7(CC[C@]9([C@]8(CC[C@@H]9CCCCCCCC)C)C)C)(CC6=N5)C)C)C)C)C)C)C
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| InChi Key |
YRQNKMKHABXEJZ-UVQQGXFZSA-N
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| InChi Code |
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
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| Chemical Name |
(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
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
H2O : ~50 mg/mL
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|---|---|
| Solubility (In Vivo) |
Note: Listed below are some common formulations that may be used to formulate products with low water solubility (e.g. < 1 mg/mL), you may test these formulations using a minute amount of products to avoid loss of samples.
Injection Formulations
Injection Formulation 1: DMSO : Tween 80: Saline = 10 : 5 : 85 (i.e. 100 μL DMSO stock solution → 50 μL Tween 80 → 850 μL Saline)(e.g. IP/IV/IM/SC) *Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH ₂ O to obtain a clear solution. Injection Formulation 2: DMSO : PEG300 :Tween 80 : Saline = 10 : 40 : 5 : 45 (i.e. 100 μL DMSO → 400 μLPEG300 → 50 μL Tween 80 → 450 μL Saline) Injection Formulation 3: DMSO : Corn oil = 10 : 90 (i.e. 100 μL DMSO → 900 μL Corn oil) Example: Take the Injection Formulation 3 (DMSO : Corn oil = 10 : 90) as an example, if 1 mL of 2.5 mg/mL working solution is to be prepared, you can take 100 μL 25 mg/mL DMSO stock solution and add to 900 μL corn oil, mix well to obtain a clear or suspension solution (2.5 mg/mL, ready for use in animals). View More
Injection Formulation 4: DMSO : 20% SBE-β-CD in saline = 10 : 90 [i.e. 100 μL DMSO → 900 μL (20% SBE-β-CD in saline)] Oral Formulations
Oral Formulation 1: Suspend in 0.5% CMC Na (carboxymethylcellulose sodium) Oral Formulation 2: Suspend in 0.5% Carboxymethyl cellulose Example: Take the Oral Formulation 1 (Suspend in 0.5% CMC Na) as an example, if 100 mL of 2.5 mg/mL working solution is to be prepared, you can first prepare 0.5% CMC Na solution by measuring 0.5 g CMC Na and dissolve it in 100 mL ddH2O to obtain a clear solution; then add 250 mg of the product to 100 mL 0.5% CMC Na solution, to make the suspension solution (2.5 mg/mL, ready for use in animals). View More
Oral Formulation 3: Dissolved in PEG400  (Please use freshly prepared in vivo formulations for optimal results.) |
Calculation results
Working concentration: mg/mL;
Method for preparing DMSO stock solution: mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation::Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O,mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.