JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB141579

SB-3CT, MMP-2 and MMP-9 inhibitor

Be the first to review this product! Submit a review

|

(3 Publications)

MW 306.4 Da, Purity >98%. Potent, competitive and non-selective MMP-2 and MMP-9 inhibitor (Ki values are 13.9 and 600 nM for MMP-2 and MMP-9 respectively). Does not alter the activity of MMP-1, MMP-3 or MMP-7 (Ki values are 206 (MMP-1), 15 (MMP-3) and 96 (MMP-7) μM). Neuroprotective and blood-brain barrier permeable.

View Alternative Names

72 kDa gelatinase, 72kD type IV collagenase, 82 kDa matrix metalloproteinase-9, 92 kDa gelatinase, 92 kDa type IV collagenase, CLG 4, CLG 4A, CLG 4B, Collagenase Type 4 alpha, Collagenase Type 4 beta, Collagenase type IV 92 KD, Collagenase type IV A, EC 3.4.24.35, GELB, Gelatinase 92 KD, Gelatinase A, Gelatinase B, Gelatinase alpha, Gelatinase beta, Gelatinase neutrophil, MANDP2, MMP II, MMP-X1, MMP14_HUMAN, MMP2_HUMAN, MMP9_HUMAN, MONA, MT-MMP 1, MT1-MMP, Macrophage gelatinase, Matrix Metalloproteinase 9, 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 metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), Matrix metalloproteinase II, Matrix metalloproteinase-14, Matrix metalloproteinase-2, Membrane type 1 metalloprotease, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, Neutrophil gelatinase, PEX, TBE-1, Type V collagenase

1 Images
Chemical Structure - SB-3CT, MMP-2 and MMP-9 inhibitor (AB141579)
  • Chemical Structure

Lab

Chemical Structure - SB-3CT, MMP-2 and MMP-9 inhibitor (AB141579)

2D chemical structure image of ab141579, SB-3CT, MMP-2 and MMP-9 inhibitor

Key facts

CAS number

292605-14-2

Purity

>98%

Form

Solid

form

Molecular weight

306.4 Da

Molecular formula

C<sub>1</sub><sub>5</sub>H<sub>1</sub><sub>4</sub>O<sub>3</sub>S<sub>2</sub>

PubChem

9883002

Nature

Synthetic

Solubility

Soluble in DMSO to 25 mM

Soluble in ethanol

Biochemical name

2-[(4-Phenoxyphenyl)sulfonylmethyl]thiirane

Biological description

Potent, competitive and non-selective MMP-2 and MMP-9 inhibitor (Ki values are 13.9 and 600 nM for MMP-2 and MMP-9 respectively). Does not alter the activity of MMP-1, MMP-3 or MMP-7 (Ki values are 206 (MMP-1), 15 (MMP-3) and 96 (MMP-7) μM). Neuroprotective and blood-brain barrier permeable.

Canonical smiles

C1C(S1)CS(=O)(=O)C2=CC=C(C=C2)OC3=CC=CC=C3

InChi

InChI=1S/C15H14O3S2/c16-20(17,11-14-10-19-14)15-8-6-13(7-9-15)18-12-4-2-1-3-5-12/h1-9,14H,10-11H2

InChiKey

LSONWRHLFZYHIN-UHFFFAOYSA-N

IUPAC Name

2-[(4-phenoxyphenyl)sulfonylmethyl]thiirane

style
left-column
style
left-column

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
style
left-column

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MMP14 also known as MT1-MMP MMP2 and MMP9 are enzymes in the matrix metalloproteinase (MMP) family which are zinc-dependent endopeptidases. They play major role in degrading extracellular matrix proteins. MMP14 has a molecular mass of about 66 kDa and is expressed in various tissues including the brain and connective tissues. MMP2 often referred as gelatinase A weighs approximately 72 kDa while MMP9 or gelatinase B is around 92 kDa. Both MMP2 and MMP9 appear in many cell types like macrophages neutrophils and fibroblasts. Their expression promotes tissue remodeling and repair.
Biological function summary

MMP14 MMP2 and MMP9 are significant in matrix remodeling processes. These proteins can form active complexes in presence of TIMPs (tissue inhibitors of metalloproteinases) regulating their activity. They break down not just structural proteins in extracellular matrix but also bioactive molecules impacting cellular functions such as migration invasion and angiogenesis. This biological activity of MMPs is critical in both physiological development and pathological processes.

Pathways

MMP14 MMP2 and MMP9 contribute significantly to the ECM-receptor interaction pathway and the PI3K-AKT signaling pathway. These pathways influence cell survival proliferation and migration. Additionally they relate to proteins like TIMP1 and TIMP2 that regulate their enzymatic activity. By integrating these pathways MMPs sustain important mechanisms in tissue homeostasis and pathological conditions such as tissue fibrosis and cancer progression.

MMP14 MMP2 and MMP9 have strong associations with cancer and arthritis. These enzymes facilitate cancer invasion and metastasis by degrading surrounding tissue barriers often seen in a range of tumorigenic processes. In arthritis particularly rheumatoid arthritis their imbalance leads to enhanced cartilage degradation. Connecting to this role in disease are proteins like cytokines and growth factors that induce MMP expression further implicating them in disease etiology and progression.
style
left-column
style
left-column

Product protocols

style
left-column

Publications (3)

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

Science advances 9:eadd9275 PubMed36989370

2023

How the mechanobiology orchestrates the iterative and reciprocal ECM-cell cross-talk that drives microtissue growth.

Applications

Unspecified application

Species

Unspecified reactive species

Mario C Benn,Simon A Pot,Jens Moeller,Tadahiro Yamashita,Charlotte M Fonta,Gertraud Orend,Philip Kollmannsberger,Viola Vogel

Biophysical journal 114:650-662 PubMed29414711

2018

MMP Secretion Rate and Inter-invadopodia Spacing Collectively Govern Cancer Invasiveness.

Applications

Unspecified application

Species

Unspecified reactive species

Sandeep Kumar,Alakesh Das,Amlan Barai,Shamik Sen

Annals of Indian Academy of Neurology 17:171-8 PubMed25024567

2014

Cerebrospinal fluid cytokines and matrix metalloproteinases in human immunodeficiency seropositive and seronegative patients of tuberculous meningitis.

Applications

Unspecified application

Species

Unspecified reactive species

Dheeraj Rai,Ravindra Kumar Garg,Abbas Ali Mahdi,Amita Jain,Rajesh Verma,Anil Kumar Tripathi,Maneesh Kumar Singh,Hardeep Singh Malhotra,Gyan Prakash Singh,Mohammad Kaleem Ahmad
View all publications
style
left-column
style
left-column
style
right-column

Complementary Products

Secondary Antibodies

AB150113

Goat Anti-Mouse IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Mouse IgG H&L (Alexa Fluor® 488) (AB150113)

  • 5
  • 15
Assay Kits

AB112146

MMP Activity Assay Kit (Fluorometric - Green)

Functional Studies - MMP Activity Assay Kit (Fluorometric - Green) (AB112146)

  • 4
  • 6
Primary Antibodies

AB9485

Anti-GAPDH antibody - Loading Control

BOND RX™ Validated|Lab Essentials

Immunocytochemistry/ Immunofluorescence - Anti-GAPDH antibody - Loading Control (AB9485)

  • 5
  • 88
Primary Antibodies

AB15580

Anti-Ki67 antibody

BOND RX™ Validated|KO Validated

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ki67 antibody (AB15580)

  • 5
  • 230

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com