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AB142087

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.

View 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, 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

1 Images
Chemical Structure - Batimastat (BB-94), Matrix metalloprotease (MMP) inhibitor (AB142087)
  • 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

Key facts

CAS number

130370-60-4

Purity

>98%

Form

Solid

form

Molecular weight

477.6 Da

Molecular formula

C<sub>2</sub><sub>3</sub>H<sub>3</sub><sub>1</sub>N<sub>3</sub>O<sub>4</sub>S<sub>2</sub>

PubChem

5362422

Nature

Synthetic

Solubility

Soluble in DMSO to 100 mM

Biochemical name

Batimastat

Biological description

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.

Canonical smiles

CC(C)CC(C(CSC1=CC=CS1)C(=O)NO)C(=O)NC(CC2=CC=CC=C2)C(=O)NC

Isomeric smiles

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

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

InChiKey

XFILPEOLDIKJHX-QYZOEREBSA-N

IUPAC Name

(2S,3R)-N-hydroxy-N'-[(2S)-1-(methylamino)-1-oxo-3-phenylpropan-2-yl]-3-(2-methylpropyl)-2-(thiophen-2-ylsulfanylmethyl)butanediamide

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months

Supplementary information

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.
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.

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.

Product protocols

Publications (9)

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

iScience 27:111424 PubMed39717087

2024

EMT-related cell-matrix interactions are linked to states of cell unjamming in cancer spheroid invasion.

Applications

Unspecified application

Species

Unspecified reactive species

Anouk van der Net,Zaid Rahman,Ankur D Bordoloi,Iain Muntz,Peter Ten Dijke,Pouyan E Boukany,Gijsje H Koenderink

The Journal of cell biology 224: PubMed39656438

2024

An eGFP-Col4a2 mouse model reveals basement membrane dynamics underlying hair follicle morphogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Duligengaowa Wuergezhen,Eleonore Gindroz,Ritsuko Morita,Kei Hashimoto,Takaya Abe,Hiroshi Kiyonari,Hironobu Fujiwara

Aging cell 22:e13744 PubMed36514868

2022

Dissecting the influence of cellular senescence on cell mechanics and extracellular matrix formation in vitro.

Applications

Unspecified application

Species

Unspecified reactive species

Erik Brauer,Tobias Lange,Daniela Keller,Sophie Görlitz,Simone Cho,Jacqueline Keye,Manfred Gossen,Ansgar Petersen,Uwe Kornak

Function (Oxford, England) 2:zqab037 PubMed34423304

2021

Matrix-Bound Growth Factors are Released upon Cartilage Compression by an Aggrecan-Dependent Sodium Flux that is Lost in Osteoarthritis.

Applications

Unspecified application

Species

Unspecified reactive species

Stuart J Keppie,Jessica C Mansfield,Xiaodi Tang,Christopher J Philp,Helen K Graham,Patrik Önnerfjord,Alanna Wall,Celia McLean,C Peter Winlove,Michael J Sherratt,Galina E Pavlovskaya,Tonia L Vincent

BioTechniques 61:323-326 PubMed27938324

2016

Analysis and quantification of in vitro myoblast fusion using the LADD Multiple Stain.

Applications

Unspecified application

Species

Unspecified reactive species

Rhys McColl,Mthokozisi Nkosi,Celia Snyman,Carola Niesler

PLoS pathogens 12:e1005848 PubMed27732661

2016

Molecular Basis of Acute Cystitis Reveals Susceptibility Genes and Immunotherapeutic Targets.

Applications

Unspecified application

Species

Unspecified reactive species

Ines Ambite,Manoj Puthia,Karoly Nagy,Caterina Cafaro,Aftab Nadeem,Daniel S C Butler,Gustav Rydström,Nina A Filenko,Björn Wullt,Thomas Miethke,Catharina Svanborg

The Journal of biological chemistry 291:21903-21912 PubMed27563067

2016

Alternative Processing of the Amyloid Precursor Protein Family by Rhomboid Protease RHBDL4.

Applications

Unspecified application

Species

Unspecified reactive species

Sandra Paschkowsky,Mehdi Hamzé,Felix Oestereich,Lisa Marie Munter

Acta diabetologica 51:1055-64 PubMed25374383

2014

Extracellular vesicles derived from mesenchymal stem cells induce features of diabetic retinopathy in vitro.

Applications

Unspecified application

Species

Unspecified reactive species

Elena Beltramo,Tatiana Lopatina,Elena Berrone,Aurora Mazzeo,Alessandra Iavello,Giovanni Camussi,Massimo Porta

Nature immunology 15:973-81 PubMed25151489

2014

B cell homeostasis and follicle confines are governed by fibroblastic reticular cells.

Applications

Unspecified application

Species

Unspecified reactive species

Viviana Cremasco,Matthew C Woodruff,Lucas Onder,Jovana Cupovic,Janice M Nieves-Bonilla,Frank A Schildberg,Jonathan Chang,Floriana Cremasco,Christopher J Harvey,Kai Wucherpfennig,Burkhard Ludewig,Michael C Carroll,Shannon J Turley
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