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Nlr Proteins: Methods and Protocols, Di Virgilio Francesco, Pelegrнn Pablo


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Автор: Di Virgilio Francesco, Pelegrнn Pablo
Название:  Nlr Proteins: Methods and Protocols
ISBN: 9781493980796
Издательство: Springer
Классификация:

ISBN-10: 1493980793
Обложка/Формат: Paperback
Страницы: 256
Вес: 0.48 кг.
Дата издания: 26.05.2018
Серия: Methods in molecular biology
Язык: English
Издание: Softcover reprint of
Иллюстрации: 38 tables, color; 8 tables, black and white; 43 illustrations, color; 9 illustrations, black and white; xi, 256 p. 52 illus., 43 illus. in color.
Размер: 25.40 x 17.78 x 1.45 cm
Читательская аудитория: General (us: trade)
Подзаголовок: Methods and protocols
Ссылка на Издательство: Link
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Поставляется из: Германии
Описание: This volume provides a sound basis for the molecular investigation of NLR function in health and disease. Chapters focus on of innate immune receptors, “atypical” inflammasomes, biochemical and novel bioluminescence techniques for the measurement of IL-1b, bioluminescent probe, biochemical and microscopy techniques, techniques to measure caspase-1 activation, cell free systems for the study of inflammasome function, and inflammasome activation. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, NLR Proteins: Methods and Protocols aims to ensure successful results in the further study of this vital field.
Дополнительное описание: Innate Immune Receptors.- Atypical Inflammasomes.- Assessment of Inflammasome Activation By Cytokine And Danger Signal Detection.- Investigating IL-1? Secretion Using Real-Time Single-Cell Imaging.- Measuring IL-1? Processing By Bioluminescence Sensors I:



Nlr proteins

Название: Nlr proteins
ISBN: 149393564X ISBN-13(EAN): 9781493935642
Издательство: Springer
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Цена: 13275.00 р.
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Описание: Chapters focus on of innate immune receptors, "atypical"inflammasomes, biochemical and novel bioluminescencetechniques for the measurement of IL-1b,bioluminescent probe, biochemical and microscopytechniques, techniques to measure caspase-1 activation, cellfree systems for the study of inflammasome function, and inflammasomeactivation.

HPLC of Peptides and Proteins / Methods and Protocols

Автор: Aguilar Marie-Isabel
Название: HPLC of Peptides and Proteins / Methods and Protocols
ISBN: 0896039773 ISBN-13(EAN): 9780896039773
Издательство: Springer
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Цена: 23757.00 р.
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Описание: Hands-on experts from academia and industry comprehensively describe how to successfully perform all the critical HPLC techniques needed for the analysis of peptides and proteins. The methods range from commonly used techniques to those for capillary to large-scale preparative isolation. The authors have also presented a number of specific applications as case studies to illustrate the analytical approaches to a particular separation or assay challenge, with examples drawn from contemporary fields in biochemistry and biotechnology.

Therapeutic Proteins / Methods and Protocols

Автор: Smales C. Mark, James David C.
Название: Therapeutic Proteins / Methods and Protocols
ISBN: 1588293904 ISBN-13(EAN): 9781588293909
Издательство: Springer
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Цена: 27950.00 р.
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Описание: World-class researchers share their innovative and proven techniques for the production of therapeutic proteins downstream of the discovery stage. The methods use a variety of sources for producing therapeutic proteins, including bacterial and yeast expression systems, and insect and mammalian cells, and then cover the purification of the resulting protein using both state-of-the-art and traditional methods, such as those sourced from plasma. Additional chapters offer methods for the characterization of therapeutic proteins throughout the production process, along with methods and strategies for viral inactivation and protein formulation. The protocols follow the successful Methods in Molecular Biologyв„ў series format, each offering step-by-step laboratory instructions, an introduction outlining the principles behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.

Immunocytochemical methods and protocols

Автор: Constance Oliver; Maria Celia Jamur (Eds.)
Название: Immunocytochemical methods and protocols
ISBN: 1588294633 ISBN-13(EAN): 9781588294630
Издательство: Springer
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Цена: 9084.00 р.
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Описание: This third edition reflects the rapid evolution of immunocytochemistry in the post-genomic era. Expert researchers explore the latest methods, now widely used in situ to identify components of cells and tissues in both normal and pathological conditions.

Serum/Plasma Proteomics: Methods and Protocols

Автор: Simpson Richard J., Greening David W.
Название: Serum/Plasma Proteomics: Methods and Protocols
ISBN: 1493958011 ISBN-13(EAN): 9781493958016
Издательство: Springer
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Цена: 20263.00 р.
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Описание: Blood science has become a cornerstone of multiple disciplines, including clinical chemistry, disease diagnosis, and therapeutic monitoring. Over the past decade, we have witnessed the advent of increasingly powerful proteomics technologies that allow greater fundamental insights into the blood proteome. These technological improvements have, in part, fuelled the quest for the discovery of novel blood-based biomarkers of disease. Serum/Plasma Proteomics: Methods and Protocols is a comprehensive resource of protocols for areas, pre-analytical through to analytical, of plasma and serum proteomics. Divided into five convenient sections, this detailed volume covers fractionation strategies for in-depth blood proteome analysis, defined procedures for blood collection, handling and storage, detailed protocols for performing both antibody-based and non-antibody based quantitative assays, proteome analysis of blood cell compartments, circulating nanomebraneous vesicles and blood-related fluids, and finally data management, statistical design, and bioinformatic challenges. This book, contributed to by leading experts in the field, provides a valuable foundation for the development and application of blood-based proteomics. 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. Authoritative and easily accessible, Serum/Plasma Proteomics: Methods and Protocols, with its well-honed methodologies, seeks to serve both professionals and investigators new to the field in an effort to further our knowledge of this fundamental science.

Immunocytochemical Methods and Protocols

Автор: Oliver
Название: Immunocytochemical Methods and Protocols
ISBN: 1617796824 ISBN-13(EAN): 9781617796821
Издательство: Springer
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Цена: 18167.00 р.
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Описание: This third edition reflects the rapid evolution of immunocytochemistry in the post-genomic era. Expert researchers explore the latest methods, now widely used in situ to identify components of cells and tissues in both normal and pathological conditions.

Phosphodiesterase Methods and Protocols

Автор: Claire Lugnier
Название: Phosphodiesterase Methods and Protocols
ISBN: 1617374873 ISBN-13(EAN): 9781617374876
Издательство: Springer
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Цена: 20263.00 р.
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Описание: Study of Cyclic Adenosine Monophosphate Microdomains in Cells Marco Mongillo, Anna Terrin, Sandrine Evellin, Valentina Lissandron, and Manuela Zaccolo High-Resolution Measurements of Cyclic Adenosine Monophosphate Signals in 3D Microdomains Jeffrey W. Karpen and Thomas C. Rich Cygnets: In Vivo Characterization of Novel cGMP Indicators and In Vivo Imaging of Intracellular cGMP Akira Honda, Carolyn L. Sawyer, Sharon M. Cawley, and Wolfgang R. G. Dostmann High-Throughput Screening of Phosphodiesterase Activity in Living Cells Thomas C. Rich and Jeffrey W. Karpen Assessment of Phosphodiesterase Isozyme Contribution in Cell and Tissue Extracts Thйrиse Keravis, Rima Thaseldar-Roumiй, and Claire Lugnier Localization of the Cyclic Guanosine 39,59-Monophosphate- Hydrolyzing Phosphodiesterase Type 9 in Rat Brain by Nonradioactive In Situ Hybridization Wilma C. G. van Staveren and Marjanne Markerink-van Ittersum Determination of Ca2+/Calmodulin-Stimulated Phosphodiesterase Activity in Intact Cells Chen Yan Adenovirus-Mediated Overexpression of Murine Cyclic Nucleotide Phosphodiesterase 3B Faiyaz Ahmad, Linda Hдrndahl, Yan Tang, Lena Stenson Holst, and Vincent C. Manganiello Identification of Promoter Elements in the 5'-Flanking Region of Murine Cyclic Nucleotide Phosphodiesterase 3B Gene Hanguan Liu, Jing Rong Tang, Eva Degerman, and Vincent C. Manganiello Purification of PDE6 Isozymes From Mammalian Retina Dana C. Pentia, Suzanne Hosier, Rachel A. Collupy, Beverly A. Valeriani, and Rick H. Cote Cyclic Guanosine 59-Monophosphate Binding to Regulatory GAF Domains of Photoreceptor Phosphodiesterase Rick H. Cote Renaturation of the Catalytic Domain of PDE4A Expressed in Escherichia coli as Inclusion Bodies Wito Richter, Thomas Hermsdorf, and Dietrich Dettmer Determining the SubunitStructure of Phosphodiesterases Using Gel Filtration and Sucrose Density Gradient Centrifugation Wito Richter Crystallization of Cyclic Nucleotide Phosphodiesterases Hengming Ke, Qing Huai, and Robert X. Xu Generation of PDE4 Knockout Mice by Gene Targeting S.-L. Catherine Jin, Anne M. Latour, and Marco Conti Immunoprecipitation of PDE2 Phosphorylated and Inactivated by an Associated Protein Kinase J. Kelley Bentley Investigation of Extracellular Signal-Regulated Kinase 2 Mitogen-Activated Protein Kinase Phosphorylation and Regulation of Activity of PDE4 Cyclic Adenosine Monophosphate-Specific Phosphodiesterases Elaine V. Hill, Miles D. Houslay, and George S. Baillie Radiolabeled Ligand Binding to the Catalytic or Allosteric Sites of PDE5 and PDE11 James L. Weeks II, Mitsi A. Blount, Alfreda Beasley, Roya Zoraghi, Melissa K. Thomas, Konjeti Raja Sekhar, Jackie D. Corbin, and Sharron H. Francis Analysis of Dimerization Determinants of the PDE6 Catalytic Subunits Khakim G. Muradov, Kimberly K. Boyd, and Nikolai O. Artemyev Interaction Between Catalytic and Inhibitory Subunits of PDE6 Nikolai O. Artemyev Purification, Reconstitution on Lipid Vesicles, and Assays of PDE6 and Its Activator G Protein, Transducin Theodore G. Wensel, Feng He, and Justine A. Malinski Index

Lipidomics: Methods and Protocols

Автор: Bhattacharya Sanjoy K.
Название: Lipidomics: Methods and Protocols
ISBN: 1493983628 ISBN-13(EAN): 9781493983629
Издательство: Springer
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Цена: 19564.00 р.
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Описание:

Preface...
Table of Contents...
Contributing Authors...

1. Lipid Sample Preparation for Biomedical Research
Ravin Sajnani and Katyayini Aribindi

2. Lipid Extraction Techniques for Stable Isotope Analysis and Ecological Assays
Kyle H. Elliot, James D. Roth, and Kevin Crook

3. Isolation of Lipid Raft Proteins from CD133+ Cancer Stem Cells
Vineet K. Gupta and Sulagna Banerjee

4. Isolation of Neuronal Synaptic Membranes by Sucrose Gradient Centrifugation
Blake E. Hopiavuori, Dustin E. Masser, Joseph L. Wilkerson, Richard S. Brush, Nawajes A. Mandal, Robert E. Anderson, and Willard M. Freeman

5. Sample Preparation and Analysis for Imaging Mass Spectrometry
Genea Edwards, Annia Mesa, Robert I. Vazquez-Padron, Paul Kowalski, and Sanjoy K. Bhattacharya

6. Direct Measurement of Free and Esterified Cholesterol Mass in Differentiated Human Podocytes: A TLC and Enzymatic Assay Based Method
Christopher E. Pedigo, Sandra M. Merscher, and Alessia Fornoni

7. High-Performance Chromatographic Separation of Cerebrosides
Renaud Sicard and Ralf Landgraf

8. Lipid Identification by Untargeted Tandem Mass Spectrometry Coupled with Ultra-High-Pressure Liquid Chromatography
Gabriel B. Gugiu

9. Utility of Moderate and High Resolution Mass Spectrometry for Class-Specific Lipid Identification and Quantification
Maria del Carmen Piqueras

10. A Robust Lipidomics Workflow for Mammalian Cells, Plasma, and Tissue using Liquid-Chromatography High-Resolution Tandem Mass Spectrometry
Candice Z. Ulmer, Rainey Patterson, Jeremy Koelmel, Timothy J. Garrett, and Richard A. Yost

11. Combined Use of MALDI-TOF Mass Spectrometry and 31PNMR Spectrometry for Analysis of Phospholipids
Jenny Schrцter, Yulia Popkova, Rosmarie Sь , and Jьrgen Schiller

12. Global Monitoring of Mammalian Lipidome by Quantitative Shotgun Lipodomics
Inger dum Nielsen, Kenji Maeda, and Mesut Bilgin

13. Bioinformatics Pertinent to Lipid Analysis in Biological Samples
Justin Ma, Ulises Arbelo, Yenifer Guerra, Katyayini Aribindi, Sanjoy K. Bhattacharya, and Daniel Pelaez

14. LC-MS-Based Lipidomics and Automated Identification of Lipids using the LipidBlast In-Silico MS/MS Library
Tomas Cajka and Oliver Fiehn

15. Single-Step Capture and Targeted Metabolomics of Alkyl-Quinolones in Outer Membrane Vesicles of Pseudomonas aeruginosa
Pallavi Lahiri and Dipankar Ghosh

16. Analysis of Fatty Acid and Cholesterol Content from Detergent-Resistant and Detergent-Free Membrane Microdomains
Mark E. McClellan and Michael H. Elliott

17. Computational Functional Analysis of Lipid Metabolic Enzymes
Carolina Bagnato, Arjen Ten Have, Marнa B. Prados, and Marнa B. Beligni

18. Isoprenylation of Monomeric GTPases in Human Trabecular Meshwork Cells
Evan B. Stubbs, Jr.

19. Purification and Validation of Lipid Transfer Proteins
Matti A. Kjellberg, Anders P.E. Backman, Anna Mцuts, and Peter Mattjus

20. Incorporation of Artificial Lipid-Anchored Proteins into Cultured Mammalian Cells
Rania Leventis and John R. Silvius

21. Sonication-Based Basic Protocol for Liposome Synthesis
Roberto Mendez and Santanu Banerjee

22. On Electrochemical Methods for Determination of Protein-Lipid Interaction
Zhiping Hu and Yanli Mao

23. Angiogenesis Model of Cornea to Understand the Role of Sphingosine 1-Phosphate
Joseph L. Wilkerson and Nawajes A. Mandal

Erk Signaling: Methods and Protocols

Автор: Jimenez Gerardo
Название: Erk Signaling: Methods and Protocols
ISBN: 1493981951 ISBN-13(EAN): 9781493981953
Издательство: Springer
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Цена: 15372.00 р.
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Описание:

1. How Genetics has Helped Piece Together the MAPK Signaling Pathway
Dariel Ashton-Beaucage and Marc Therrien

2. In Vitro Enzyme Kinetics Analysis of EGFR
Zhihong Wang and Christine Candelora


3. High-Throughput Analysis of Mammalian Receptor Tyrosine Kinase Activation in Yeast Cells
Nobuo Yoshimoto and Shun'ichi Kuroda

4. Structural Studies of ERK2 Protein Complexes
Johannes F. Weijman, Stefan J. Riedl, and Peter D. Mace

5. Isolation and Characterization of Intrinsically Active (MEK-Independent) Mutants of Mpk1/Erk
Tal Goshen-Lago, Dganit Melamed, Arie Admon, and David Engelberg

6. Assaying Activation and Subcellular Localization of ERK in Cells and Tissues
Carme Caelles, Carles Bayod, and Melisa Morcillo

7. Detection and Functional Analysis of SUMO-Modified MEK
Yuji Kubota and Mutsuhiro Takekawa

8. Single-Step Affinity Purification of ERK Signaling Complexes Using the Streptavidin-Binding Peptide (SBP) Tag
Liu Yang and Alexey Veraksa

9. High-Throughput In Vitro Identification of Direct MAPK/Erk Substrates
Rona Grossman and Ze'ev Paroush

10. Global Identification of ERK Substrates by Phosphoproteomics Based on IMAC and 2D-DIGE
Hidetaka Kosako and Kou Motani

11. Analysis of Ras/ERK Compartmentalization by Subcellular Fractionation
Lorena Agudo-Ibaсez, Piero Crespo, and Berta Casar

12. Cell-Based Assays to Study ERK Pathway/Caveolin1 Interactions
Raffaele Strippoli, Asier Echarri, Miguel Angel del Pozo

13. The Nuclear Translocation of ERK
Denise A. Berti and Rony Seger

14. Visualization of RAS/MAPK Signaling In Situ by the Proximity Ligation Assay (PLA)
Zijian Tang and Chengkai Dai

15. Measuring ERK Activity Dynamics in Single Living Cells Using FRET Biosensors
Yannick Blum, Rafael D. Fritz, Hyunryul Ryu, and Olivier Pertz

16. Quantifying Tensile Force and ERK Phosphorylation on Actin Stress Fibers
Hiroaki Hirata, Mukund Gupta, Sri Ram Krishna Vedula, Chwee Teck Lim, Benoit Ladoux, and Masahiro Sokabe

17. Co-Culture Activation of MAP Kinase in Drosophila S2 Cells
Josefa Steinhauer

18. Isolation of Mouse Embryonic Stem Cell Lines in the Study of ERK1/2 MAP Kinase Signaling
Marc K. Saba-El-Leil, Christophe Frйmin, and Sylvain Meloche

19. 3D Organotypic Culture Model to Study Components of ERK Signaling
Athina-Myrto Chioni, Rabia Tayba Bajwa, and Richard Grose

20. Genetic Validation of Cell Proliferation via Ras-Independent Activation of the Raf/Mek/Erk Pathway
Carmen G. Lechuga, Lucнa Simуn-Carrasco, Harrys K.C. Jacob, and Matthias Drosten

21. Genome-Wide Analysis of RAS/ERK Signaling Targets
Joshua P. Plotnik and Peter C. Hollenhorst

22. Probing Chromatin Modifications in Response to ERK Signaling
Ozgur Oksuz and Wee-Wei Tee

23. Analyzing pERK Activation during Planarian Regeneration
Susanna Fraguas, Yoshihiko Umesono, Kiyokazu Agata, and Francesc Cebriа
24. Discovering Functional ERK Substrates Regulating Caenorhabditis elegans Germline Development
Jessica Jie Chen and Swathi Arur

25. Reconstructing ERK Signaling in the Drosophila Embryo from Fixed Images
Bomyi Lim, Carmeline J. Dsilva, Ioannis G. Kevrekidis, and Stanislav Y. Shvartsman

Protein Synthesis: Methods and Protocols

Автор: Bhupendra Pushkar
Название: Protein Synthesis: Methods and Protocols
ISBN: 1774077035 ISBN-13(EAN): 9781774077030
Издательство: Mare Nostrum (Eurospan)
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Цена: 22730.00 р.
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Описание: Takes readers through the various ways in which proteins are synthesized and then further used for other applications. The book throws light on chemical reactions taking place in the process, and lays down different kinds of methods and the procedures that are followed in protein synthesis.

Matrix Metalloproteases: Methods and Protocols

Автор: Galea Charles A.
Название: Matrix Metalloproteases: Methods and Protocols
ISBN: 1493983210 ISBN-13(EAN): 9781493983216
Издательство: Springer
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Цена: 16070.00 р.
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Описание:

PART I Expression and Purification of Matrix Metalloproteases

1. Expression and Purification of Matrix Metalloproteinases in Escherichia coli

Krishna K. Singh, Ruchi Jain, Harini Ramanan, and Deepak K. Saini

2. Expression and Purification of a Matrix Metalloprotease Transmembrane Domain in Escherichia coli

Charles A. Galea

3. Heterologous Expression of the Astacin Protease Meprin b in Pichia pastoris

Dagmar Schlenzig and Stephan Schilling

PART II Structural Characterization of Matrix Metalloproteases

4. Structural Studies of Matrix Metalloproteinase by X-Ray Diffraction

Elena Decaneto, Wolfgang Lubitz, and Hideaki Ogata

5. Mapping Lipid Bilayer Recognition Sites of Metalloproteinases and other Prospective Peripheral Membrane Proteins

Tara C. Marcink, Rama K. Koppisetti, Yan G. Fulcher, and Steven R. Van Doren

6. Using Small Angle X-ray Scattering (SAXS) to Characterise the Solution Conformation and Flexibility of Matrix Metalloproteinases (MMPs)

Louise E. Butt, Robert A. Holland, Nikul S. Khunti, Debra L. Quinn, and Andrew R. Pickford

PART III Computational Simulations of Matrix Metalloproteases

7. Molecular Dynamics Studies of Matrix Metalloproteases

Natalia Dнaz and Dimas Suбrez

PART IV Determining Matrix Metalloprotease Substrate Specificity

8. Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates

Maciej J. Stawikowski, Anna M. Knapinska, and Gregg B. Fields

9. Time-resolved Analysis of Matrix Metalloproteinase Substrates in Complex Samples

Pascal Schlage, Fabian E. Egli, and Ulrich auf dem Keller

10. Identification of Protease Cleavage Sites by Charge-Based Enrichment of Protein N-termini

Zon W. Lai and Oliver Schilling

11. Mapping the Substrate Recognition Landscapes of Metalloproteases using Comprehensive Mutagenesis

Colin A. Kretz

PART V Detection of Matrix Metalloproteases

12. Detection of Matrix Metalloproteinases by Zymography

Rajeev B. Tajhya, Rutvik S. Patel, and Christine Beeton

13. Imaging Matrix Metalloproteases in Spontaneous Colon Tumors: Validation by Correlation with Histopathology

Harvey Hensley, Harry S. Cooper, Wen-Chi L. Chang, and Margie L. Clapper

PART VI Matrix Metalloprotease Inhibitors 14. Virtual High-throughput Screening for Matrix Metalloproteinase Inhibitors Jun Yong Choi, and Rita Fuerst

15. Computational Approaches to Matrix Metalloprotease Drug Design

Tanya Singh, B. Jayaram, and Olayiwola Adedotun Adekoya

16. A Simple, Adaptable Blood-Brain Barrier Cell Model for Screening Matrix Metalloproteinase Inhibitor Functionality

Jennifer S. Myers, Joan Hare, and Qing-Xiang Amy Sang

PART VII Matrix Metalloproteases as Biomarkers

17. Matrix Metalloproteases as Biomarkers of Disease

Fernando Luiz Affonso Fonseca, Beatriz da Costa Aguiar Alves, Ligia Ajaime Azzalis, and Thaнs Moura Gбscon Belardo


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