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AB139449

MMP9 Inhibitor Screening Assay Kit (Fluorometric)

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(1 Publication)

Abcam MMP9 Inhibitor Screening Assay Kit (Fluorometric) (ab139449) is a complete assay system designed to screen MMP9 inhibitors using a quenched fluorogenic peptide: MMP Fluorogenic Substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 [Mca=(7-methoxycoumarin-4-yl)-acetyl; Dpa=N-3-(2,4-dinitrophenyl)-L-α-β-diaminopropionyl].

View Alternative Names

CLG4B, MMP9, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB

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Functional Studies - MMP9 Inhibitor Screening Assay Kit (Fluorometric) (AB139449)
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Supplier Data

Functional Studies - MMP9 Inhibitor Screening Assay Kit (Fluorometric) (AB139449)

Example of Inhibitor Data.

Inhibiton of MMP9 by NNGH.

Key facts

Detection method

Fluorescent

Sample types

Inhibitor compounds

Assay type

Enzyme activity

Assay Platform

Microplate reader

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Enzyme activity assay": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Abcam MMP9 Inhibitor Screening Assay Kit (Fluorometric) (ab139449) is a complete assay system designed to screen MMP9 inhibitors using a quenched fluorogenic peptide: MMP Fluorogenic Substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 [Mca=(7-methoxycoumarin-4-yl)-acetyl; Dpa=N-3-(2,4-dinitrophenyl)-L-α-β-diaminopropionyl]. Mca fluorescence is quenched by the Dpa group until cleavage by MMPs at the Gly-Leu bond separates the two moieties. The assays are performed in a convenient 96-well microplate format.

This kit is useful to screen inhibitors of MMP9, a potential therapeutic target. The MMP inhibitor NNGH is also included as a prototypic control inhibitor.

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What's included?

{ "values": { "1x96Tests": { "sellingSize": "1 x 96 Tests", "publicAssetCode":"ab139449-1x96Tests", "assetComponentDetails": [ { "size":"1 x 1 Unit", "name":"96-well White Microplate 1/2 Volume", "number":"AB139449-CMP06", "productcode":"" }, { "size":"1 x 48.5 µL", "name":"MMP9 Enzyme (Human, Recombinant)", "number":"AB139449-CMP01", "productcode":"" }, { "size":"1 x 50 µL", "name":"MMP Calibration Standard", "number":"AB139449-CMP02", "productcode":"" }, { "size":"1 x 20 mL", "name":"Fluorometric Assay Buffer", "number":"AB139449-CMP05", "productcode":"" }, { "size":"1 x 50 µL", "name":"MMP Inhibitor", "number":"AB139449-CMP04", "productcode":"" }, { "size":"1 x 200 µL", "name":"MMP Fluorogenic Substrate", "number":"AB139449-CMP03", "productcode":"" } ] } } }
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
Multi
Storage information
Please refer to protocols
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Supplementary information

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

The MMP-9 protein also known as matrix metalloproteinase-9 or gelatinase B functions as an enzyme involved in the breakdown of extracellular matrix proteins. It consists of a zinc ion at its active site and facilitates the degradation of type IV and V collagens fibronectin and elastin. MMP-9 has a molecular weight of approximately 92 kDa and is expressed in a variety of tissues including the liver lungs and immune cells. This enzyme can exist in monomer and dimer forms with its activity regulated by tissue inhibitors of metalloproteinases (TIMPs).
Biological function summary

Matrix metalloproteinase-9 profoundly influences tissue remodeling inflammation and angiogenesis. It does not form part of a larger protein complex but interacts closely with substrates in the extracellular matrix. MMP-9 plays important roles in processes such as embryogenesis reproduction and wound healing through the remodeling of surrounding tissues. The MMP-9 protein is often measured using assays like ELISA or analyzed via techniques such as Western blotting to determine its expression levels and activity in different biological contexts.

Pathways

MMP-9 participates in the matrix metalloproteinase pathway and the NF-kB signaling pathway. These pathways are essential in orchestrating processes such as tissue remodeling and inflammatory responses. MMP-9 acts alongside other matrix metalloproteinases including MMP-2 and is regulated by factors like cytokines growth factors and hormones ensuring the precision of extracellular matrix degradation during physiological processes.

Matrix metalloproteinase-9 has associations with cancer invasion and metastasis as well as chronic inflammatory diseases like rheumatoid arthritis. In cancer upregulated MMP-9 expression aids tumor cells in breaching the basement membrane facilitating metastasis. The disorder-associated pathways often involve interactions with proteins like vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta). Understanding MMP-9's role in these conditions can contribute to developing targeted therapies that inhibit its activity potentially mitigating disease progression.
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Product protocols

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Target data

The protein expressed by gene MMP9 is a matrix metalloproteinase that plays an essential role in the local proteolysis of the extracellular matrix and in leukocyte migration. It cleaves KiSS1 at a Gly-|-Leu bond and processes NINJ1 to generate the Secreted ninjurin-1 form. Additionally, MMP9 cleaves type IV and type V collagen into large C-terminal three-quarter fragments and shorter N-terminal one-quarter fragments. It degrades fibronectin but not laminin or Pz-peptide. This supplementary information is collated from multiple sources and compiled automatically.
See full target information MMP9
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Publications (1)

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

International journal of molecular sciences 24: PubMed37108137

2023

Carborane-Containing Hydroxamate MMP Ligands for the Treatment of Tumors Using Boron Neutron Capture Therapy (BNCT): Efficacy without Tumor Cell Entry.

Applications

Unspecified application

Species

Unspecified reactive species

Sebastian Flieger,Mao Takagaki,Natsuko Kondo,Marlon R Lutz,Yash Gupta,Hiroki Ueda,Yoshinori Sakurai,Graham Moran,Prakasha Kempaiah,Narayan Hosmane,Minoru Suzuki,Daniel P Becker
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