MW 477.6 Da, Purity >98%. Potent, broad-spectrum MMP inhibitor (IC50 values are 3 (MMP-1), 4 (MMP-2), 4 (MMP-9), 6 (MMP-7), 20 nM (MMP-3)). Anticancer activity in vivo.
Also available as a solid (ab142087).
130370-60-4
> 98%
Solid
477.6 Da
C23H31N3O4S2
5362422
Synthetic
27 kDa interstitial collagenase, 72 kDa gelatinase, 72kD type IV collagenase, 82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, BLAST-2, C-type lectin domain family 4, C-type lectin domain family 4 member J, CD 23, CD 23A, CD23 antigen, CHDS6, CLEC 4J, CLG, CLG 3, CLG 4, CLG 4A, CLG 4B, Collagenase 3, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, EC 3.4.24.35, FCE 2, FCER2A, FCER2_HUMAN, Fc epsilon receptor II, Fc fragment of IgE, Fc fragment of IgE low affinity II receptor for, Fc fragment of IgE receptor II, Fc fragment of IgE, low affinity II, receptor for (CD23), Fc of IgE, Fc of IgE, low affinity II, receptor for (CD23), Fc receptor IgE low affinity II alpha polypeptide, Fc receptor, IgE, low affinity II, alpha polypeptide, isoform CRA_a, Fc-epsilon-RII, FceRII, Fibroblast collagenase, GELB, Gelatinase 92 KD, Gelatinase A, Gelatinase B, Gelatinase alpha, Gelatinase beta, Gelatinase neutrophil, IGEBF, IgE receptor lymphocyte, IgE-binding factor, Immunoglobulin E receptor, Immunoglobulin E receptor, low affinity II, Immunoglobulin E-binding factor, Immunoglobulin epsilon chain, Interstitial collagenase, LEUKOCYTE ANTIGEN CD23, Low Affinity IgE Receptor, Low affinity immunoglobulin epsilon Fc receptor, Low affinity immunoglobulin epsilon Fc receptor membrane bound form, Low affinity immunoglobulin epsilon Fc receptor soluble form, Ly-42, Lymphocyte IgE receptor, Lymphocyte antigen CD23, MANDP1, MANDP2, MGC126102, MGC126103, MGC126104, MGC93219, MMP II, MMP-X1, MMP13_HUMAN, MMP14_HUMAN, MMP1_HUMAN, MMP2_HUMAN, MMP3_HUMAN, MMP7_HUMAN, MMP9_HUMAN, MONA, MPSL1, MT-MMP 1, MT1-MMP, Macrophage gelatinase, Matrilysin, Matrin, Matrix Metalloproteinase 9, Matrix metallopeptidase 1 (interstitial collagenase), Matrix metallopeptidase 13 (collagenase 3), Matrix metallopeptidase 14 (membrane inserted), Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase, Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase), Matrix metalloprotease 1, Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), Matrix metalloproteinase 3 preproprotein, Matrix metalloproteinase II, Matrix metalloproteinase-1, Matrix metalloproteinase-13, Matrix metalloproteinase-14, Matrix metalloproteinase-2, Matrix metalloproteinase-3, Matrix metalloproteinase-7, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, Neutrophil gelatinase, OTTHUMP00000045866, PEX, PUMP 1, Proteoglycanase, Pump-1 protease, SL-1, STMY, STMY1, Stromelisin 1, Stromelysin 1 progelatinase, Stromelysin-1, TBE-1, Transin-1, Type V collagenase, Uterine matrilysin, Uterine metalloproteinase, collagenase, fibroblast, collagenase, interstitial
MW 477.6 Da, Purity >98%. Potent, broad-spectrum MMP inhibitor (IC50 values are 3 (MMP-1), 4 (MMP-2), 4 (MMP-9), 6 (MMP-7), 20 nM (MMP-3)). Anticancer activity in vivo.
Also available as a solid (ab142087).
130370-60-4
> 98%
Solid
477.6 Da
C23H31N3O4S2
5362422
Synthetic
Batimastat
Potent, broad-spectrum MMP inhibitor (IC50 values are 3 (MMP-1), 4 (MMP-2), 4 (MMP-9), 6 (MMP-7), 20 nM (MMP-3)). Anticancer activity in vivo.
Also available as a solid (ab142087).
CC(C)CC(C(CSC1=CC=CS1)C(=O)NO)C(=O)NC(CC2=CC=CC=C2)C(=O)NC
CC(C)C[C@H]([C@H](CSC1=CC=CS1)C(=O)NO)C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)NC
InChI=1S/C23H31N3O4S2/c1-15(2)12-17(18(22(28)26-30)14-32-20-10-7-11-31-20)21(27)25-19(23(29)24-3)13-16-8-5-4-6-9-16/h4-11,15,17-19,30H,12-14H2,1-3H3,(H,24,29)(H,25,27)(H,26,28)/t17-,18+,19+/m1/s1
XFILPEOLDIKJHX-QYZOEREBSA-N
(2S,3R)-N-hydroxy-N'-[(2S)-1-(methylamino)-1-oxo-3-phenylpropan-2-yl]-3-(2-methylpropyl)-2-(thiophen-2-ylsulfanylmethyl)butanediamide
Ambient - Can Ship with Ice
-20°C
-20°C
Store under desiccating conditions, The product can be stored for up to 12 months
This supplementary information is collated from multiple sources and compiled automatically.
MMP14 MMP1 MMP2 MMP3 MMP9 MMP13 and MMP7 collectively known as matrix metalloproteinases (MMPs) are enzymes important for the breakdown of extracellular matrix proteins. MMP14 also called MT1-MMP is a membrane-type MMP with a mass of approximately 66 kDa and is often found on the cell surface. MMP1 known as interstitial collagenase weighs around 54 kDa and is expressed in fibroblasts and keratinocytes. MMP2 or gelatinase A is about 72 kDa and is secreted by fibroblasts and endothelial cells. MMP3 also known as stromelysin 1 has a mass of approximately 54 kDa and is detected in connective tissues. MMP9 or gelatinase B is 92 kDa and expressed by neutrophils and macrophages. MMP13 sometimes referred to as collagenase 3 weighs around 60 kDa and is expressed in chondrocytes. MMP7 also called matrilysin is around 28 kDa and expressed in epithelial cells.
Matrix metalloproteinases influence tissue remodeling and wound healing processes. They do this by degrading structural components like collagen and elastin controlling the turnover and reconstruction of the matrix. These enzymes do not act alone; they often form complexes with tissue inhibitors of metalloproteinases (TIMPs) to regulate their activities and maintain tissue integrity. MMPs facilitate cellular migration in inflammation and angiogenesis by modulating the extracellular environment ensuring proper tissue development and repair.
These MMPs integrate into processes such as the extracellular matrix degradation pathway and the angiogenesis pathway. They interact dynamically with proteins like TIMP-1 and TIMP-2 which modulate their proteolytic activity. Matrix metalloproteinases help release matrix-bound growth factors affecting pathways that proliferate and differentiate cells during tissue repair and remodeling.
Elevated levels of matrix metalloproteinases often correlate with cancer progression and arthritis. They contribute to cancer metastasis by degrading the basal membrane aiding tumor cell invasion. MMPs also play significant roles in joint destruction in rheumatoid arthritis through continuous breakdown of cartilage matrix. In these contexts MMP2 and MMP9 are often implicated working alongside other proteases in disease pathogenesis.
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2D chemical structure image of ab142087, Batimastat (BB-94), Matrix metalloprotease (MMP) inhibitor
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