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AB211108

Collagenase Inhibitor Assay Kit (Fluorometric)

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(13 Publications)

Collagenase Inhibitor Screening Kit (Fluorometric) (ab211108) provides a quick, sensitive and reliable test for high-throughput screening of collagenase inhibitors.

Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.

View Alternative Names

CLG, Fibroblast collagenase, Matrix metallopeptidase 1 (interstitial collagenase), matrix metallopeptidase 1

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Functional Studies - Collagenase Inhibitor Assay Kit (Fluorometric) (AB211108)
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Supplier Data

Functional Studies - Collagenase Inhibitor Assay Kit (Fluorometric) (AB211108)

Collagenase Inhibitor Screening Kit (ab211108). Typical inhibition curve of Collagenase activity by collagenase inhibitor. IC50 of (1,10)-Phenanthroline was determine to be 110.5 μM. Assay was performed following the kit protocol.

Key facts

Detection method

Fluorescent

Sample types

Inhibitor compounds

Assay type

Semi-quantitative

Assay Platform

Microplate reader

Reactivity data

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Product details

Collagenase Inhibitor Screening Kit (Fluorometric) (ab211108) provides a quick, sensitive and reliable test for high-throughput screening of collagenase inhibitors. The assay uses self-quenched BODIPY conjugate of Gelatin (Type B) as a fluorogenic substrate to monitor the activity of Collagenase. Upon proteolytic digestion of the highly quenched BODIPY-labeled gelatin by Collagenase, the de-quenched BODIPY yields bright green fluorescence that can be assayed using a fluorescence microplate reader at Ex/Em = 490/520 nm (515 nm cutoff). In the presence of a collagenase inhibitor, the gelatin is not digested, the dequenching of BODIPY does not occur and the fluorescent signal is not produced.

This kit can be used to screen/study/characterize potential inhibitors of Collagenase.

Other Notes
This product was previously called K833 Biovision Collagenase Inhibitor Screening Kit (Fluorometric). Biovision was acquired by Abcam in 2021.

Collagenase (EC 3.4.24.3) is an enzyme in the matrix metalloproteinase (MMP) family that breaks down collagen, assisting in degradation of the extracellular matrix, a key step in the pathogenesis of bacteria and tumor cell invasion. Collagen is an abundant structural protein present in the connective tissue of animals. Collagenase has been used clinically for the treatment of Dupuytren's contracture, an affliction characterized by a thickening of connective tissue.

The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

What's included?

{ "values": { "100Test": { "sellingSize": "100 Test", "publicAssetCode":"ab211108-100Test", "assetComponentDetails": [ { "size":"1 x 1 Vial", "name":"Collagenase Substrate (Gelatin)", "number":"AB211108-CMP04", "productcode":"" }, { "size":"1 x 30 µL", "name":"Active Collagenase", "number":"AB211108-CMP02", "productcode":"" }, { "size":"1 x 25 mL", "name":"Assay Buffer 38", "number":"AB211108-CMP03", "productcode":"" }, { "size":"1 x 50 µL", "name":"Collagenase Inhibitor", "number":"AB211108-CMP01", "productcode":"" } ] } } }

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Collagenase refers to a group of enzymes capable of breaking down collagen an important structural protein in the extracellular matrix. These enzymes including matrix metalloproteinase (MMP) family members like MMP-1 (also known as fibroblast collagenase) have molecular weights typically around 50-60 kDa. Collagenase enzymes can be expressed in various tissues such as skin cartilage and bone and also in fibroblasts and inflammatory cells. They play a significant role in remodeling and degrading extracellular matrix components which is essential for processes like tissue repair and development.
Biological function summary

These enzymes participate in collagen degradation allowing for cellular migration and growth by clearing path through the dense collagen network. Collagenase activity is carefully regulated because uncontrolled activity can lead to tissue damage and diseases. The enzymes do not function alone; they often form complexes or interact with inhibitors such as tissue inhibitors of metalloproteinases (TIMPs) which maintain the necessary balance in matrix remodeling. Researchers utilize collagenase inhibition assay techniques to study these interactions as well as to gauge enzyme efficiency and control.

Pathways

Collagenase enzymes significantly contribute to the pathways of tissue remodeling and wound healing. They are involved in the matrix metalloproteinase pathway working with other MMPs like MMP-2 and MMP-9. In these pathways they collaborate with proteins such as elastase and stromelysin to degrade various matrix components. Balance between collagenase and TIMP proteins regulates these processes ensuring that tissue integrity is maintained during dynamic changes in the body.

Excessive collagenase activity connects to arthritic disease and tumor metastasis. In arthritis there is an overproduction of collagenase particularly in joints which leads to the excessive breakdown of cartilage. Increased collagenase activity results as well in cancerous tumors enabling them to invade neighboring tissues. Various therapies target the regulation of collagenase and TIMP activity to mitigate tissue destruction and inhibit cancer progression.

Product protocols

Publications (13)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 25: PubMed38892121

2024

New Polymeric Hydrogels with Cannabidiol and α-Terpineol as Potential Materials for Skin Regeneration-Synthesis and Physicochemical and Biological Characterization.

Applications

Unspecified application

Species

Unspecified reactive species

Martyna Zagórska-Dziok,Anna Nowak,Anna Zgadzaj,Ewa Oledzka,Karolina Kędra,Agnieszka Ewa Wiącek,Marcin Sobczak

International journal of molecular sciences 24: PubMed37686038

2023

Comparative Study of Cytotoxicity and Antioxidant, Anti-Aging and Antibacterial Properties of Unfermented and Fermented Extract of L.

Applications

Unspecified application

Species

Unspecified reactive species

Martyna Zagórska-Dziok,Aleksandra Ziemlewska,Agnieszka Mokrzyńska,Zofia Nizioł-Łukaszewska,Ireneusz Sowa,Dariusz Szczepanek,Magdalena Wójciak

Molecules (Basel, Switzerland) 28: PubMed36677923

2023

Phenolic Profile and Comparison of the Antioxidant, Anti-Ageing, Anti-Inflammatory, and Protective Activities of Extracts on Skin Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Monika Michalak,Martyna Zagórska-Dziok,Marta Klimek-Szczykutowicz,Agnieszka Szopa

Molecules (Basel, Switzerland) 27: PubMed35565960

2022

A New Xanthone Glycoside from L.: Physicochemical Properties and In Vitro Anti-Skin Aging Activities.

Applications

Unspecified application

Species

Unspecified reactive species

Heba A S El-Nashar,Eman M El-Labbad,Mahmood A Al-Azzawi,Naglaa S Ashmawy

Molecules (Basel, Switzerland) 27: PubMed35408743

2022

Evaluation of Cosmetic and Dermatological Properties of Kombucha-Fermented Berry Leaf Extracts Considered to Be By-Products.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandra Ziemlewska,Zofia Nizioł-Łukaszewska,Martyna Zagórska-Dziok,Tomasz Bujak,Magdalena Wójciak,Ireneusz Sowa

Molecules (Basel, Switzerland) 27: PubMed35164187

2022

Flower Extracts as Multifunctional Dyes in the Cosmetics Industry.

Applications

Unspecified application

Species

Unspecified reactive species

Tomasz Bujak,Martyna Zagórska-Dziok,Aleksandra Ziemlewska,Zofia Nizioł-Łukaszewska,Kamila Lal,Tomasz Wasilewski,Zofia Hordyjewicz-Baran

Scientific reports 11:18792 PubMed34552134

2021

Effect of fermentation time on the content of bioactive compounds with cosmetic and dermatological properties in Kombucha Yerba Mate extracts.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandra Ziemlewska,Zofia Nizioł-Łukaszewska,Tomasz Bujak,Martyna Zagórska-Dziok,Magdalena Wójciak,Ireneusz Sowa

Molecules (Basel, Switzerland) 26: PubMed34200200

2021

L. Extracts as Valuable Ingredients in Cosmetic and Dermatological Products.

Applications

Unspecified application

Species

Unspecified reactive species

Anna Nowak,Martyna Zagórska-Dziok,Paula Ossowicz-Rupniewska,Edyta Makuch,Wiktoria Duchnik,Łukasz Kucharski,Urszula Adamiak-Giera,Piotr Prowans,Norbert Czapla,Piotr Bargiel,Jan Petriczko,Marta Markowska,Adam Klimowicz

Molecules (Basel, Switzerland) 26: PubMed34068613

2021

Antioxidant and Cytoprotective Properties of Plant Extract from Dry Flowers as Functional Dyes for Cosmetic Products.

Applications

Unspecified application

Species

Unspecified reactive species

Tomasz Bujak,Martyna Zagórska-Dziok,Aleksandra Ziemlewska,Zofia Nizioł-Łukaszewska,Tomasz Wasilewski,Zofia Hordyjewicz-Baran

Molecules (Basel, Switzerland) 26: PubMed33557174

2021

Positive Effect of L. Herb Extracts on Skin Cells and Assessment of Cannabinoid-Based Hydrogels Properties.

Applications

Unspecified application

Species

Unspecified reactive species

Martyna Zagórska-Dziok,Tomasz Bujak,Aleksandra Ziemlewska,Zofia Nizioł-Łukaszewska
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