Batimastat (BB-94), Matrix metalloprotease (MMP) inhibitor
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(9 Publications)
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.
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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
- Chemical Structure
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Chemical Structure - Batimastat (BB-94), Matrix metalloprotease (MMP) inhibitor (AB142087)
2D chemical structure image of ab142087, Batimastat (BB-94), Matrix metalloprotease (MMP) inhibitor
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Publications (9)
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iScience 27:111424 PubMed39717087
2024
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The Journal of cell biology 224: PubMed39656438
2024
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Aging cell 22:e13744 PubMed36514868
2022
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Function (Oxford, England) 2:zqab037 PubMed34423304
2021
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BioTechniques 61:323-326 PubMed27938324
2016
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PLoS pathogens 12:e1005848 PubMed27732661
2016
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The Journal of biological chemistry 291:21903-21912 PubMed27563067
2016
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Acta diabetologica 51:1055-64 PubMed25374383
2014
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Nature immunology 15:973-81 PubMed25151489
2014
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