MMP14/MT1-MMP Rabbit Pab

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Leader in Biomolecular Solutions for Life Science MMP14/MT1-MMP Rabbit pAb Catalog No.: A2549 3 Publications Basic Information Background Catalog No. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of A2549 extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis Observed MW and metastasis. Most MMP's are secreted as inactive proproteins which are activated 46-70kDa when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this Calculated MW subfamily contains a potential transmembrane domain suggesting that these proteins 65kDa are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. Category Primary antibody Applications WB, IHC Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 4323 P50281 IHC 1:50 - 1:100 Immunogen Recombinant protein of human MMP14/MMP14/MT1-MMP Synonyms MMP14;MMP-14;MMP-X1;MT-MMP;MT-MMP 1;MT1- MMP;MT1MMP;MTMMP1;WNCHRS;MT-MMP1 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using MMP14/MMP14/MT1-MMP antibody (A2549) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 90s. Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- embedded rat kidney using embedded human kidney using MMP14/MMP14/MT1-MMP antibody MMP14/MMP14/MT1-MMP antibody (A2549) at dilution of 1:100 (40x lens). (A2549) at dilution of 1:100 (40x lens). Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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Discovery and Optimization of Selective Inhibitors of Meprin Α (Part II)
pharmaceuticals Article Discovery and Optimization of Selective Inhibitors of Meprin α (Part II) Chao Wang 1,2, Juan Diez 3, Hajeung Park 1, Christoph Becker-Pauly 4 , Gregg B. Fields 5 , Timothy P. Spicer 1,6, Louis D. Scampavia 1,6, Dmitriy Minond 2,7 and Thomas D. Bannister 1,2,* 1 Department of Molecular Medicine, Scripps Research, Jupiter, FL 33458, USA; [email protected] (C.W.); [email protected] (H.P.); [email protected] (T.P.S.); [email protected] (L.D.S.) 2 Department of Chemistry, Scripps Research, Jupiter, FL 33458, USA; [email protected] 3 Rumbaugh-Goodwin Institute for Cancer Research, Nova Southeastern University, 3321 College Avenue, CCR r.605, Fort Lauderdale, FL 33314, USA; [email protected] 4 The Scripps Research Molecular Screening Center, Scripps Research, Jupiter, FL 33458, USA; [email protected] 5 Unit for Degradomics of the Protease Web, Institute of Biochemistry, University of Kiel, Rudolf-Höber-Str.1, 24118 Kiel, Germany; fi[email protected] 6 Department of Chemistry & Biochemistry and I-HEALTH, Florida Atlantic University, 5353 Parkside Drive, Jupiter, FL 33458, USA 7 Dr. Kiran C. Patel College of Allopathic Medicine, Nova Southeastern University, 3301 College Avenue, Fort Lauderdale, FL 33314, USA * Correspondence: [email protected] Abstract: Meprin α is a zinc metalloproteinase (metzincin) that has been implicated in multiple diseases, including fibrosis and cancers. It has proven difficult to find small molecules that are capable Citation: Wang, C.; Diez, J.; Park, H.; of selectively inhibiting meprin α, or its close relative meprin β, over numerous other metzincins Becker-Pauly, C.; Fields, G.B.; Spicer, which, if inhibited, would elicit unwanted effects.
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Transmembrane/Cytoplasmic, Rather Than Catalytic, Domains of Mmp14
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Self-Organization of Engineered Epithelial Tubules by Differential Cellular Motility
Self-organization of engineered epithelial tubules by differential cellular motility Hidetoshi Moria,1, Nikolce Gjorevskib,1, Jamie L. Inmana,1, Mina J. Bissella,2, and Celeste M. Nelsonb,2 aLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; and bDepartments of Chemical Engineering and Molecular Biology, Princeton University, Princeton, NJ 08544 Edited by Kenneth Yamada, National Institutes of Health, Bethesda, MD, and accepted by the Editorial Board July 16, 2009 (received for review February 4, 2009) Patterning of developing tissues arises from a number of mecha- also in many epithelial tumors, including those from breast, lung, nisms, including cell shape change, cell proliferation, and cell sorting and colon (17–19), and confers cancer cells with the pernicious from differential cohesion or tension. Here, we reveal that differences ability to degrade and penetrate the basement membrane and in cell motility can also lead to cell sorting within tissues. Using mosaic metastasize to distant sites (20–23). Intriguingly, cells at the invasive engineered mammary epithelial tubules, we found that cells sorted front of metastatic cohorts express the highest levels of MMP14 (24, depending on their expression level of the membrane-anchored 25). Understanding how the expression pattern of this protease is collagenase matrix metalloproteinase (MMP)-14. These rearrange- determined will likely yield insights into possible mechanisms of ments were independent of the catalytic activity of MMP14 but cancer progression and invasion. absolutely required the hemopexin domain. We describe a signaling Here we present evidence to suggest that cellular rearrange- cascade downstream of MMP14 through Rho kinase that allows cells ments generated by differential cellular motility determine the to sort within the model tissues.
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MMP14 Gene Matrix Metallopeptidase 14
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Proteolytic Cleavage—Mechanisms, Function
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Human MMP14 / MT1-MMP Assay Kit (ARG82633)
Product datasheet [email protected] ARG82633 Package: 96 wells Human MMP14 / MT1-MMP Assay Kit Store at: -20°C Summary Product Description ARG82633 Human MMP14 / MT1-MMP Assay Kit is a detection kit for the quantification of Human MMP14 in cell and tissue lysates. Tested Reactivity Hu Tested Application FuncSt Specificity Measures endogenous active MMP14 (naturally occurring). Target Name MMP14 / MT1-MMP Conjugation Note Read at 405 nm. Sensitivity 500 pg/ml for 2 hours incubation 100 pg/ml for 5 hours incubation Sample Type Cell and tissue lysates Standard Range 100 - 16000 pg/ml Sample Volume 100 µl Alternate Names MT1MMP; MT-MMP 1; Membrane-type matrix metalloproteinase 1; MT1-MMP; Membrane-type-1 matrix metalloproteinase; MT-MMP; EC 3.4.24.80; MMP-X1; MMP-14; Matrix metalloproteinase-14; WNCHRS; MTMMP1 Application Instructions Assay Time Overnight Properties Form 96 well Storage instruction Store the kit at -20°C. Keep microplate wells sealed in a dry bag with desiccants. Do not expose test reagents to heat, sun or strong light during storage and usage. Please refer to the product user manual for detail temperatures of the components. Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol MMP14 Gene Full Name matrix metallopeptidase 14 (membrane-inserted) Background Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.
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NEDD9 Depletion Leads to MMP14 Inactivation by TIMP2 and Prevents Invasion and Metastasis
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© 2019. Published by The Company of Biologists Ltd | Journal of Cell Science (2019) 132, jcs220665. doi:10.1242/jcs.220665 RESEARCH ARTICLE The cancer-associated meprin β variant G32R provides an additional activation site and promotes cancer cell invasion Henning Schäffler1, Wenjia Li4, Ole Helm2, Sandra Krüger3, Christine Böger3, Florian Peters1, Christoph Röcken3, Susanne Sebens2, Ralph Lucius4, Christoph Becker-Pauly1 and Philipp Arnold4,* ABSTRACT Thus, a well-balanced ratio of shed and membrane-bound meprin β The extracellular metalloprotease meprin β is expressed as a is required for a specific cellular function. β homodimer and is primarily membrane bound. Meprin β can be Meprin displays a unique cleavage preference for negatively released from the cell surface by its known sheddases ADAM10 and charged amino acids around the scissile bond (Becker-Pauly et al., ADAM17. Activation of pro-meprin β at the cell surface prevents its 2011), and has been shown to play important roles for proper shedding, thereby stabilizing its proteolytic activity at the plasma collagen I maturation in the skin and for the mucus detachment in membrane. We show that a single amino acid exchange variant the small intestine (Wichert et al., 2017; Broder et al., 2013; Schutte β (G32R) of meprin β, identified in endometrium cancer, is more active et al., 2014). Increased levels of meprin have been found in fibrotic against a peptide substrate and the IL-6 receptor than wild-type meprin conditions of the skin and lung (Becker-Pauly et al., 2007; Biasin β β. We demonstrate that the change to an arginine residue at position 32 et al., 2014).
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Selective Blockade of Matrix Metalloprotease-14 with a Monoclonal Antibody Abrogates Invasion, Angiogenesis, and Tumor Growth in Ovarian Cancer
Published OnlineFirst February 19, 2013; DOI: 10.1158/0008-5472.CAN-12-1426 Cancer Microenvironment and Immunology Research Selective Blockade of Matrix Metalloprotease-14 with a Monoclonal Antibody Abrogates Invasion, Angiogenesis, and Tumor Growth in Ovarian Cancer Rajani Kaimal1, Raid Aljumaily1,2, Sarah L. Tressel1, Rutika V. Pradhan1, Lidija Covic1,2,5, Athan Kuliopulos1,2,5, Corrine Zarwan6, Young B. Kim3, Sheida Shariﬁ4,7, and Anika Agarwal1,2 Abstract Most patients with ovarian cancer are diagnosed late in progression and often experience tumor recurrence and relapses due to drug resistance. Surface expression of matrix metalloprotease (MMP)-14 on ovarian cancer cells stimulates a tumor–stromal signaling pathway that promotes angiogenesis and tumor growth. In a cohort of 92 patients, we found that MMP-14 was increased in the serum of women with malignant ovarian tumors. Therefore, we investigated the preclinical efﬁcacy of a MMP-14 monoclonal antibody that could inhibit the migratory and invasive properties of aggressive ovarian cancer cells in vitro. MMP-14 antibody disrupted ovarian tumor–stromal communication and was equivalent to Avastin in suppressing blood vessel growth in mice harboring Matrigel plugs. These effects on angiogenesis correlated with downregulation of several important angiogenic factors. Furthermore, mice with ovarian cancer tumors treated with anti–MMP-14 monotherapy showed a marked and sustained regression in tumor growth with decreased angiogenesis compared with immunoglobulin G (IgG)-treated controls. In a model of advanced peritoneal ovarian cancer, MMP-14–dependent invasion and metastasis was effectively inhibited by intraperitoneal administration of monoclonal MMP-14 antibody. Together, these studies provide a preclinical proof-of-concept for MMP-14 targeting as an adjuvant treatment strategy for advanced ovarian cancer.
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Figure S1. GO Analysis of Genes in Glioblastoma Cases That Showed Positive and Negative Correlations with TCIRG1 in the GSE16011 Cohort
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