MW 388.5 Da, Purity >98%. Broad spectrum potent MMP inhibitor. Ki values are 0.4 (MMP-1), 0.5 (MMP-2), 27 (MMP-3), 0.1 (MMP-8), 0.2 (MMP-9), 13.4 (MMP-14) and 0.36 (MMP-26) nM. IC50 value for MMP-7 is 3.7 nM. Pharmacologically active in vivo.
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- Development, growth & differentiation 66:133-1442024Macrophages enhance regeneration of lateral line neuromast derived from interneuromast cells through TGF-β in zebrafish.Applications:Unspecified applicationReactive species:Unspecified reactive speciesWei-Lin Hsu,Yu-Chi Lin,Meng-Ju Lin,Yi-Wen Wang,Shyh-Jye LeePubMed 38281811
- iScience 26:1082112023Syndecan-1 shedding destroys epithelial adherens junctions through STAT3 after renal ischemia/reperfusion injury.Applications:Unspecified applicationReactive species:Unspecified reactive speciesMan Guo,Daoqi Shen,Yiqi Su,Jiarui Xu,Shuan Zhao,Weidong Zhang,Yaqiong Wang,Wuhua Jiang,Jialin Wang,Xuemei Geng,Xiaoqiang Ding,Xialian XuPubMed 37942007
- Scientific reports 13:155082023A 3D adrenocortical carcinoma tumor platform for preclinical modeling of drug response and matrix metalloproteinase activity.Applications:Unspecified applicationReactive species:Unspecified reactive speciesPriya H Dedhia,Hemamylammal Sivakumar,Marco A Rodriguez,Kylie G Nairon,Joshua M Zent,Xuguang Zheng,Katie Jones,Liudmila V Popova,Jennifer L Leight,Aleksander SkardalPubMed 37726363
- Journal of molecular cell biology 14:2023The regenerative response of cardiac interstitial cells.Applications:Unspecified applicationReactive species:Unspecified reactive speciesLaura Rolland,Alenca Harrington,Adèle Faucherre,Jourdano Mancilla Abaroa,Girisaran Gangatharan,Laurent Gamba,Dany Severac,Marine Pratlong,Thomas Moore-Morris,Chris JoplingPubMed 36271843
- Science advances 9:eadd92752023How the mechanobiology orchestrates the iterative and reciprocal ECM-cell cross-talk that drives microtissue growth.Applications:Unspecified applicationReactive species:Unspecified reactive speciesMario C Benn,Simon A Pot,Jens Moeller,Tadahiro Yamashita,Charlotte M Fonta,Gertraud Orend,Philip Kollmannsberger,Viola VogelPubMed 36989370
- Acta biomaterialia 155:167-1812022Self-assembly of mesoscale collagen architectures and applications in 3D cell migration.Applications:Unspecified applicationReactive species:Unspecified reactive speciesChang Liu,Ryan Y Nguyen,Gabriela A Pizzurro,Xingjian Zhang,Xiangyu Gong,Alejandro Rossello Martinez,Michael MakPubMed 36371004
- Journal of biomedical materials research. Part A 111:389-4032022Click chemistry functionalization of self-assembling peptide hydrogels.Applications:Unspecified applicationReactive species:Unspecified reactive speciesJoe T Sharick,Angelina J Atieh,Keith J Gooch,Jennifer L LeightPubMed 36210776
- Nature communications 13:11512022Changes to gut amino acid transporters and microbiome associated with increased E/I ratio in Chd8 mouse model of ASD-like behavior.Applications:Unspecified applicationReactive species:Unspecified reactive speciesYou Yu,Bing Zhang,Peifeng Ji,Zhenqiang Zuo,Yongxi Huang,Ning Wang,Chang Liu,Shuang-Jiang Liu,Fangqing ZhaoPubMed 35241668
- Science advances 7:eabj68952021Discovery of anti-inflammatory physiological peptides that promote tissue repair by reinforcing epithelial barrier formation.Applications:Unspecified applicationReactive species:Unspecified reactive speciesYukako Oda,Chisato Takahashi,Shota Harada,Shun Nakamura,Daxiao Sun,Kazumi Kiso,Yuko Urata,Hitoshi Miyachi,Yoshinori Fujiyoshi,Alf Honigmann,Seiichi Uchida,Yasushi Ishihama,Fumiko ToyoshimaPubMed 34788088
- Molecular neurobiology 58:5703-57212021Dolutegravir Inhibition of Matrix Metalloproteinases Affects Mouse Neurodevelopment.Applications:Unspecified applicationReactive species:Unspecified reactive speciesAditya N Bade,JoEllyn M McMillan,Yutong Liu,Benson J Edagwa,Howard E GendelmanPubMed 34390469
Key facts
- CAS number
- 142880-36-2
- Purity
- > 98%
- Form
- Solid
- Molecular weight
- 388.5 Da
- Molecular formula
- C20H28N4O4
- PubChem identifier
- 132519
- Nature
- Synthetic
Associated Products
Select an associated product type
1 product for Alternative Version
Target data
Alternative names
27 kDa interstitial collagenase, 72 kDa gelatinase, 72kD type IV collagenase, 82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, AI503551, C8orf57, CHDS6, CLG, CLG 1, CLG 3, CLG 4, CLG 4A, CLG 4B, Collagenase 1, Collagenase 1 neutrophil, Collagenase 3, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, DKFZp761D112, EC 3.4.24.35, EC 3.4.24.65, Endometase, Fibroblast collagenase, GELB, Gelatinase 92 KD, Gelatinase A, Gelatinase B, Gelatinase alpha, Gelatinase beta, Gelatinase neutrophil, HME, HNC, Interstitial collagenase, MANDP1, MANDP2, ME, MGC126102, MGC126103, MGC126104, MGC138506, MME, MMP II, MMP-X1, MMP-X2, MMP12_HUMAN, MMP13_HUMAN, MMP14_HUMAN, MMP15_HUMAN, MMP16_HUMAN, MMP17_HUMAN, MMP1_HUMAN, MMP2_HUMAN, MMP3_HUMAN, MMP7_HUMAN, MMP8_HUMAN, MMP9_HUMAN, MONA, MPSL1, MT-MMP 1, MT-MMP 2, MT-MMP 3, MT-MMP 4, MT1-MMP, MT2-MMP, MT3-MMP, MT4-MMP, Macrophage elastase, Macrophage gelatinase, Macrophage metalloelastase, Macrophage metaloelastase, Matrilysin, Matrilysin 2, Matrin, Matrix Metalloproteinase 26, Matrix Metalloproteinase 9, Matrix metallopeptidase 1 (interstitial collagenase), Matrix metallopeptidase 12 (macrophage elastase), Matrix metallopeptidase 13 (collagenase 3), Matrix metallopeptidase 14 (membrane inserted), Matrix metallopeptidase 15 membrane inserted, Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase, Matrix metallopeptidase 8 (neutrophil collagenase), Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase), Matrix metalloprotease 1, Matrix metalloprotease 12, Matrix metalloprotease 8, Matrix metalloproteinase 17 membrane inserted, Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), Matrix metalloproteinase 3 preproprotein, Matrix metalloproteinase II, Matrix metalloproteinase-1, Matrix metalloproteinase-12, Matrix metalloproteinase-13, Matrix metalloproteinase-14, Matrix metalloproteinase-15, Matrix metalloproteinase-16, Matrix metalloproteinase-17, Matrix metalloproteinase-2, Matrix metalloproteinase-3, Matrix metalloproteinase-7, Matrix metalloproteinase-8, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type matrix metalloproteinase 2, Membrane-type matrix metalloproteinase 3, Membrane-type matrix metalloproteinase 4, Membrane-type-1 matrix metalloproteinase, Membrane-type-2 matrix metalloproteinase, Membrane-type-3 matrix metalloproteinase, Membrane-type-4 matrix metalloproteinase, Neutrophil collagenase, Neutrophil gelatinase, OTTHUMP00000045866, PEX, PMNL collagenase, PMNL-CL, PUMP 1, Proteoglycanase, Pump-1 protease, Putative transmembrane protein C8orf57, SL-1, SMCP-2, STMY, STMY1, Stromelisin 1, Stromelysin 1 progelatinase, Stromelysin-1, TBE-1, Transin-1, Type V collagenase, Uterine matrilysin, Uterine metalloproteinase, collagenase, fibroblast, collagenase, interstitial
Recommended products
MW 388.5 Da, Purity >98%. Broad spectrum potent MMP inhibitor. Ki values are 0.4 (MMP-1), 0.5 (MMP-2), 27 (MMP-3), 0.1 (MMP-8), 0.2 (MMP-9), 13.4 (MMP-14) and 0.36 (MMP-26) nM. IC50 value for MMP-7 is 3.7 nM. Pharmacologically active in vivo.
Key facts
- CAS number
- 142880-36-2
- Purity
- > 98%
- Form
- Solid
- Molecular weight
- 388.5 Da
- Molecular formula
- C20H28N4O4
- PubChem identifier
- 132519
- Nature
- Synthetic
- Solubility
Soluble in DMSO to 100 mM.
- Biochemical name
- Ilomastat
- Biological description
Broad spectrum potent MMP inhibitor. Ki values are 0.4 (MMP-1), 0.5 (MMP-2), 27 (MMP-3), 0.1 (MMP-8), 0.2 (MMP-9), 13.4 (MMP-14) and 0.36 (MMP-26) nM. IC50 value for MMP-7 is 3.7 nM. Pharmacologically active in vivo.
- Canonical SMILES
- CC(C)CC(CC(=O)NO)C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC
- Isomeric SMILES
- CC(C)C[C@H](CC(=O)NO)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)NC
- InChI
- InChI=1S/C20H28N4O4/c1-12(2)8-13(10-18(25)24-28)19(26)23-17(20(27)21-3)9-14-11-22-16-7-5-4-6-15(14)16/h4-7,11-13,17,22,28H,8-10H2,1-3H3,(H,21,27)(H,23,26)(H,24,25)/t13-,17+/m1/s1
- InChIKey
- NITYDPDXAAFEIT-DYVFJYSZSA-N
- IUPAC name
- (2R)-N'-hydroxy-N-[(2S)-3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
Storage
- Shipped at conditions
- Ambient - Can Ship with Ice
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- +4°C
- Storage information
- The product can be stored for up to 12 months
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
MMPs (Matrix Metalloproteinases) such as MMP1 MMP2 MMP3 MMP7 MMP8 MMP9 MMP12 MMP13 MMP14 MMP16 MT2-MMP MT4-MMP and MMP26 are enzymes that play roles in tissue remodeling and are known for degrading extracellular matrix proteins. They are often referred to as collagenases or gelatinases depending on their substrate specificity. MMPs originate from diverse tissues including the skin lung and connective tissues and they have wide-ranging molecular masses typically between 20 to 100 kDa. They can be expressed in response to cytokines growth factors and physical stress indicating their versatile roles across different tissue environments.
- Biological function summary
MMPs facilitate the breakdown of extracellular matrix components impacting processes such as angiogenesis wound healing and embryonic development. They often work in concert with other proteins in the extracellular space potentially forming complexes with tissue inhibitors of metalloproteinases (TIMPs) which regulate their activity. MMPs not only maintain normal physiological function but also reactivate and remodel tissue structure during pathological conditions providing grounds for cellular migration and proliferation.
- Pathways
MMPs operate within significant biological processes like the inflammatory response and cellular signaling pathways including the MAPK and NF-kB pathways. They interact with other proteins such as integrins and cytokines to modulate cellular and inflammatory responses. Such interactions impact the balance between matrix formation and degradation exemplifying their involvement in tissue homeostasis and response to injury or disease.
- Associated diseases and disorders
MMPs play roles in conditions such as cancer metastasis and chronic inflammatory diseases like rheumatoid arthritis. During cancer progression MMPs such as MMP2 and MMP9 facilitate tumor invasion and the spread of cancer cells by breaking down basement membranes and stromal tissues. In arthritis MMPs lead to cartilage degradation causing joint damage. MMP inhibitors such as GM6001 have been explored to target these diseases by moderating excessive MMP activity presenting therapeutic potential for conditions exacerbated by uncontrolled proteolysis.
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Chemical Structure - GM 6001, MMP inhibitor (ab120845)
2D chemical structure image of ab120845, GM 6001, MMP inhibitor
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