MMP26 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science MMP26 Rabbit pAb Catalog No.: A16135 Basic Information Background Catalog No. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of A16135 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. The encoded preproprotein is proteolytically processed to generate the 20kDa mature enzyme. This enzyme may degrade collagen type IV, fibronectin, fibrinogen, and beta-casein, and activate matrix metalloproteinase-9 by cleavage. The protein differs Calculated MW from most MMP family members in that it lacks a conserved C-terminal protein domain. 29kDa The encoded protein may promote cell invasion in multiple human cancers. Category Primary antibody Applications WB Cross-Reactivity Mouse Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 56547 Q9NRE1 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 90-261 of human MMP26 (NP_068573.2). Synonyms MMP26 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 mouse kidney, using MMP26 antibody (A16135) 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: 30s. 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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2335 Roles of Molecules Involved in Epithelial/Mesenchymal Transition
[Frontiers in Bioscience 13, 2335-2355, January 1, 2008] Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis Giulio Ghersi Dipartimento di Biologia Cellulare e dello Sviluppo, Universita di Palermo, Italy TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Extracellular matrix 3.1. ECM and integrins 3.2. Basal lamina components 4. Cadherins. 4.1. Cadherins in angiogenesis 5. Integrins. 5.1. Integrins in angiogenesis 6. Focal adhesion molecules 7. Proteolytic enzymes 7.1. Proteolytic enzymes inhibitors 7.2. Proteolytic enzymes in angiogenesis 8. Perspective 9. Acknowledgements 10. References 1.ABSTRACT 2. INTRODUCTION Formation of vessels requires “epithelial- Growth of new blood vessels (angiogenesis) mesenchymal” transition of endothelial cells, with several plays a key role in several physiological processes, such modifications at the level of endothelial cell plasma as vascular remodeling during embryogenesis and membranes. These processes are associated with wound healing tissue repair in the adult; as well as redistribution of cell-cell and cell-substrate adhesion pathological processes, including rheumatoid arthritis, molecules, cross talk between external ECM and internal diabetic retinopathy, psoriasis, hemangiomas, and cytoskeleton through focal adhesion molecules and the cancer (1). Vessel formation entails the “epithelial- expression of several proteolytic enzymes, including matrix mesenchymal” transition of endothelial cells (ECs) “in metalloproteases and serine proteases. These enzymes with vivo”; a similar phenotypic exchange can be induced “in their degradative action on ECM components, generate vitro” by growing ECs to low cell density, or in “wound molecules acting as activators and/or inhibitors of healing” experiments or perturbing cell adhesion and angiogenesis. The purpose of this review is to provide an associated molecule functions.
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Anti-MMP26 (GW21139)
3050 Spruce Street, Saint Louis, MO 63103 USA Tel: (800) 521-8956 (314) 771-5765 Fax: (800) 325-5052 (314) 771-5757 email: [email protected] Product Information Anti-MMP26 antibody produced in chicken, affinity isolated antibody Catalog Number GW21139 Formerly listed as GenWay Catalog Number 15-288-21139, Matrix metalloproteinase-26 Antibody. – Storage Temperature Store at 20 °C The product is a clear, colorless solution in phosphate buffered saline, pH 7.2, containing 0.02% sodium azide. Synonyms: Matrix metalloproteinase 26 preproprotein, EC 3.4.24.-; MMP-26; Matrilysin-2; Endometase Species Reactivity: Human Product Description Tested Applications: WB May hydrolyze collagen type IV. fibronectin. fibrinogen. Recommended Dilutions: Recommended starting dilution beta-casein. type I gelatin and alpha-1 proteinase inhibitor. for Western blot analysis is 1:500, for tissue or cell staining Is also able to activates progelatinase B. Proteins of the 1:200. matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological Note: Optimal concentrations and conditions for each processes. such as embryonic development. reproduction. application should be determined by the user. and tissue remodeling. as well as in disease processes. such Precautions and Disclaimer as arthritis and metastasis. Most MMP's are secreted as This product is for R&D use only, not for drug, household, or inactive proproteins which are activated when cleaved by other uses. Due to the sodium azide content a material extracellular proteinases. The enzyme encoded by this gene safety data sheet (MSDS) for this product has been sent to degrades type IV collagen, fibronectin, fibrinogen, and the attention of the safety officer of your institution.
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MIAMI UNIVERSITY The Graduate School Certificate for Approving the Dissertation We hereby approve the Dissertation of Fan Meng Candidate for the Degree DOCTOR OF PHILOSOPHY ______________________________________ Director Dr. Michael W. Crowder ______________________________________ Dr. David L. Tierney ______________________________________ Dr. Carole Dabney-Smith ______________________________________ Dr. Christopher A. Makaroff ______________________________________ Graduate School Representative Dr. Hai-Fei Shi ABSTRACT BIOCHEMICAL CHARACTERIZATION AND ZINC BINDING GROUP (ZBGS) INHIBITION STUDIES ON THE CATALYTIC DOMAINS OF MMP7 (CDMMP7) AND MMP16 (CDMMP16) by Fan Meng Matrix metalloproteinase 7 (MMP7/matrilysin-1) and membrane type matrix metalloproteinase 16 (MMP16/MT3-MMP) have been implicated in the progression of pathological events, such as cancer and inflammatory diseases; therefore, these two MMPs are considered as viable drug targets. In this work, we (a) provide a review of the role(s) of MMPs in biology and of the previous efforts to target MMPs as therapeutics (Chapter 1), (b) describe our efforts at over-expression, purification, and characterization of the catalytic domains of MMP7 (cdMMP7) and MMP16 (cdMMP16) (Chapters 2 and 3), (c) present our efforts at the preparation and initial spectroscopic characterization of Co(II)-substituted analogs of cdMMP7 and cdMMP16 (Chapters 2 and 3), (d) present inhibition data on cdMMP7 and cdMMP16 using zinc binding groups (ZBG) as potential scaffolds for future inhibitors (Chapter 3), and (e) summarize our data in the context of previous results and suggest future directions (Chapter 4). The work described in this dissertation integrates biochemical (kinetic assays, inhibition studies, limited computational methods), spectroscopic (CD, UV-Vis, 1H-NMR, fluorescence, and EXAFS), and analytical (MALDI-TOF mass spectrometry, isothermal calorimetry) methods to provide a detailed structural and mechanistic view of these MMPs.
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