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Matrix Metalloproteinase Protocols / edited by Ian M. Clark.

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Holman Biotech Commons QH506 .M45 v.1 (1984)-v.20 (1993),v.22 (1994),v.24 (1994)-v.53 (1996), v.42 (1995) and v.51 (1995) reported missing 3-13-2000 v.55 (1995),v.58 (1996)-v.63 (1997), v.65 (1996)-v.154 (2001), v.156 (2001)-190 (2002), v.192 (2002)-v.407 (2007) v.409 (2007)-v.416 (2008),v.418 (2008)-v.466 v.468-v.490,v.492,v.494,v.496-499 501-506,508,510-512,514,516-517,519-536 538,540-569,571 573-589,591-608,610-615,617,620-627,630-633,636,638,642
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Format:
Book
Contributor:
Clark, Ian M., editor.
SpringerLink (Online service)
Series:
Methods in Molecular Biology, Methods and Protocols, 1064-3745 ; 622.
Springer Protocols (Springer-12345)
Methods in Molecular Biology, Methods and Protocols, 1064-3745 ; 622
Language:
English
Subjects (All):
Life sciences.
Science.
Biochemistry.
Enzymology.
Life Sciences.
Biochemistry, general.
Science, general.
Local Subjects:
Life Sciences.
Biochemistry, general.
Science, general.
Enzymology.
Physical Description:
1 online resource (XII, 472 pages).
Contained In:
Springer eBooks
Place of Publication:
Totowa, NJ : Humana Press : Imprint: Humana Press, 2010.
System Details:
text file PDF
Summary:
Since the discovery of a collagen-degrading protease in the tadpole tail in 1962, matrix metalloproteinase research has led to the discovery of more than twenty distinct vertebrate MMPs, along with a variety of homologues from diverse organisms such as the sea urchin, plants, insects, and nematode worms. Fully updating and adding to the popular first edition, Matrix Metalloproteinase Protocols, Second Edition includes a series of state-of-the-art techniques provided by eminent experts in the field. Beginning with a brief overview of the MMP arena, from how these enzymes fit into the larger degradome to what occurs when their expression and function in the mouse is modulated, the volume continues with sections on the expression and purification of MMPs and TIMPs, the detection of MMPs and TIMPs at both the protein and mRNA level, and our ability to assay MMP and TIMP activities in a wide variety of circumstances. Written in the highly successful Methods in Molecular Biology™ series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls. Comprehensive and cutting-edge, Matrix Metalloproteinase Protocols, Second Edition is an ideal source for many of the essential laboratory techniques for both novice and seasoned researchers alike collected in one convenient volume.
Contents:
MMPs and TIMPs: An Overview
Metalloproteases and the Degradome
Mouse Models of MMP and TIMP Function
Expression and Purification of MMPs and TIMPs
Expression of Recombinant MMP-28 in Mammalian Cells
Expression of Recombinant Matrix Metalloproteinases in Escherichia coli
Expression of Recombinant ADAMTS in Insect Cells
Expression and Purification of Membrane-Type MMPs
Refolding of TIMP-2 from Escherichia coli Inclusion Bodies
Purification of MMPs and TIMPs
Detection of MMPs and TIMPs
Real-Time PCR Expression Profiling of MMPs and TIMPs
Analysis of the Degradome with the CLIP-CHIP™ Microarray
In Situ Hybridization for Metalloproteinases and Their Inhibitors
Immunohistochemistry of MMPs and TIMPs
Single Nucleotide Polymorphism Genotyping in MMP Genes: The 5? Nuclease Assay
Assay of MMP and TIMP Activities
Methods for Studying Activation of Matrix Metalloproteinases
Assay of Matrix Metalloproteinases Against Matrix Substrates
Zymography and Reverse Zymography for Detecting MMPs and TIMPs
In Situ Zymography
Near-Infrared Optical Proteolytic Beacons for In Vivo Imaging of Matrix Metalloproteinase Activity
Neoepitope Antibodies Against MMP-Cleaved and Aggrecanase-Cleaved Aggrecan
In Vitro Model of Cartilage Degradation
Immunoassays for Collagenase-Mediated Cleavage of Type I and II Collagens
Collagen Degradation Assays
Analysis of MMP-Dependent Cell Migration and Invasion
Using Fluorogenic Peptide Substrates to Assay Matrix Metalloproteinases
Kinetic Analysis of the Inhibition of Matrix Metalloproteinases: Lessons from the Study of Tissue Inhibitors of Metalloproteinases
Identification of Cellular MMP Substrates Using Quantitative Proteomics: Isotope-Coded Affinity Tags (ICAT) and Isobaric Tags for Relative and Absolute Quantification (iTRAQ)
Mechanism-Based Profiling of MMPs.
Other Format:
Printed edition:
ISBN:
9781603272995
Access Restriction:
Restricted for use by site license.

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