MW 316.38 Da, Purity >98%. MMP3 (Stromelysin-1) inhibitor. Additionally shows broad spectrum inhibition activity at other MMPs. Cell permeable.
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- Translational oncology 14:1012212021Targeting matrix metalloproteinase MMP3 greatly enhances oncolytic virus mediated tumor therapy.Applications:Unspecified applicationReactive species:Unspecified reactive speciesMinglong Liang,Jian Wang,Chuanjian Wu,Manman Wu,Jingping Hu,Jianfeng Dai,Hang Ruan,Sidong Xiong,Chunsheng DongPubMed 34530193
- Neuroscience 200:199-2102011Spinal matrix metalloproteinase 3 mediates inflammatory hyperalgesia via a tumor necrosis factor-dependent mechanism.Applications:Unspecified applicationReactive species:Unspecified reactive speciesC A Christianson,B L Fitzsimmons,J-H Shim,A Agrawal,S M Cohen,X-Y Hua,T L YakshPubMed 22056600
- The Journal of biological chemistry 285:16444-522010Matrix metalloproteinase-3 is increased and participates in neuronal apoptotic signaling downstream of caspase-12 during endoplasmic reticulum stress.Applications:Unspecified applicationReactive species:Unspecified reactive speciesEun-Mee Kim et. al.PubMed 20368330
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 12:1197-2062007Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.Applications:Unspecified applicationReactive species:Unspecified reactive speciesLuis A Alcaraz,Lucia Banci,Ivano Bertini,Francesca Cantini,Antonio Donaire,Leonardo GonnelliPubMed 17710450
Key facts
- CAS number
161314-17-6
- Purity
> 98%
- Form
Solid
- Molecular weight
316.38 Da
- Molecular formula
C13H20N2O5S
- PubChem identifier
448002
- Nature
Synthetic
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, A disintegrin and metalloproteinase domain 17, A disintegrin and metalloproteinase domain 17 (tumor necrosis factor, alpha, converting enzyme), ADA17_HUMAN, ADAM 17, ADAM metallopeptidase domain 17, ADAM17 protein, CD 156b, CD156b antigen, CHDS6, CLG, CLG 1, CLG 3, CLG 4, CLG 4A, CLG 4B, CSVP, Collagenase 1, Collagenase 1 neutrophil, Collagenase 3, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, Disintegrin and metalloproteinase domain-containing protein 17, EC 3.4.24.35, EC 3.4.24.65, 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, MGC71942, MME, MMP II, MMP-X1, MMP12_HUMAN, MMP13_HUMAN, MMP14_HUMAN, MMP1_HUMAN, MMP2_HUMAN, MMP3_HUMAN, MMP7_HUMAN, MMP8_HUMAN, MMP9_HUMAN, MONA, MPSL1, MT-MMP 1, MT1-MMP, Macrophage elastase, Macrophage gelatinase, Macrophage metalloelastase, Macrophage metaloelastase, Matrilysin, Matrin, 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 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 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-2, Matrix metalloproteinase-3, Matrix metalloproteinase-7, Matrix metalloproteinase-8, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, NISBD, NISBD1, Neutrophil collagenase, Neutrophil gelatinase, OTTHUMP00000045866, PEX, PMNL collagenase, PMNL-CL, PUMP 1, Proteoglycanase, Pump-1 protease, SL-1, STMY, STMY1, Snake venom-like protease, Stromelisin 1, Stromelysin 1 progelatinase, Stromelysin-1, TACE, TBE-1, TNF-alpha convertase, TNF-alpha-converting enzyme, Transin-1, Tumor Necrosis Factor Alpha Converting Enzyme, Type V collagenase, Uterine matrilysin, Uterine metalloproteinase, collagenase, fibroblast, collagenase, interstitial
Recommended products
MW 316.38 Da, Purity >98%. MMP3 (Stromelysin-1) inhibitor. Additionally shows broad spectrum inhibition activity at other MMPs. Cell permeable.
Key facts
- CAS number
161314-17-6
- Purity
> 98%
- Form
Solid
- Molecular weight
316.38 Da
- Molecular formula
C13H20N2O5S
- PubChem identifier
448002
- Nature
Synthetic
- Solubility
Soluble in DMSO to 100 mM. Soluble in ethanol to 25 mM.
- Biochemical name
N-Isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid
- Biological description
MMP3 (Stromelysin-1) inhibitor. Additionally shows broad spectrum inhibition activity at other MMPs. Cell permeable.
- Canonical SMILES
CC(C)CN(CC(=O)NO)S(=O)(=O)C1=CC=C(C=C1)OC
- InChI
InChI=1S/C13H20N2O5S/c1-10(2)8-15(9-13(16)14-17)21(18,19)12-6-4-11(20-3)5-7-12/h4-7,10,17H,8-9H2,1-3H3,(H,14,16)
- InChIKey
JIRXORZYIXSWOB-UHFFFAOYSA-N
- IUPAC name
N-hydroxy-2-[(4-methoxyphenyl)sulfonyl-(2-methylpropyl)amino]acetamide
Storage
- Shipped at conditions
Ambient - Can Ship with Ice
- Appropriate short-term storage conditions
Ambient
- Appropriate long-term storage conditions
Ambient
- 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
Matrix metalloproteases (MMPs) are a group of zinc-dependent enzymes known for their ability to degrade extracellular matrix components. Notable members of this family include MMP14 MMP1 MMP2 MMP3 MMP9 MMP13 MMP7 MMP8 and MMP12 as well as the ADAM17 which serves similar functions. Some of these proteases such as MMP1 and MMP9 are widely expressed in various tissues such as connective epithelial and endothelial tissues. Each of these proteases has a specific molecular weight; for instance MMP9 has an approximate molecular weight of 92 kDa. MMP inhibitors regulate these enzymes preventing excessive degradation of the extracellular matrix which helps maintain tissue structure.
- Biological function summary
Matrix metalloproteases play a role in tissue remodeling wound healing and the inflammatory response. These enzymes collaborate in complexes that manage extracellular matrix degradation ensuring proper tissue repair and remodeling. MMP7 also called matrilysin has a role in processing bioactive molecules. ADAM17 known as TACE (Tumor Necrosis Factor-Alpha-Converting Enzyme) regulates the shedding of cell surface proteins that affect cell signaling and communication. Inhibiting specific MMPs helps control excessive matrix degradation representing an important function in maintaining cellular environments.
- Pathways
The functions of matrix metalloproteases extend into processes like the cytokine signaling pathway and the cell-matrix adhesion pathway. MMP9 and other MMPs facilitate the release of cytokines growth factors and cell surface receptors which are central to immune responses and cell migration. Links between these proteases and proteins such as tissue inhibitors of metalloproteinases (TIMPs) balance matrix degradation and synthesis. This regulation is critical for maintaining homeostasis and proper tissue architecture.
- Associated diseases and disorders
Chronic overexpression or dysregulation of matrix metalloproteases associates with conditions like osteoarthritis and cancer. MMP13 and MMP9 show increased activity in osteoarthritic tissue contributing to cartilage degradation. In cancer MMPs promote tumor progression and metastasis through extracellular matrix restructuring. ADAM17 involves in cancer as its role in cytokine shedding impacts cancer cell communication and proliferation. Targeting specific MMPs with inhibitors provides potential therapeutic strategies for these diseases aiming to halt pathological tissue breakdown and tumor progression.
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Chemical Structure - NNGH, Matrix metalloprotease (MMP) inhibitor (ab141259)
2D chemical structure image of ab141259, NNGH, Matrix metalloprotease (MMP) inhibitor
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