Prince / Calderwood | Molecular Chaperones | Buch | 978-1-61779-294-6 | sack.de

Buch, Englisch, Band 787, 321 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 838 g

Reihe: Methods in Molecular Biology

Prince / Calderwood

Molecular Chaperones

Methods and Protocols
2011
ISBN: 978-1-61779-294-6
Verlag: Humana Press

Methods and Protocols

Buch, Englisch, Band 787, 321 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 838 g

Reihe: Methods in Molecular Biology

ISBN: 978-1-61779-294-6
Verlag: Humana Press


The proteome consists of a complex mixture of proteins each of which need to be folded correctly in order to function for the health of the organism, and many of these proteins require molecular chaperones to reach the correct conformation and, in some cases, to remain in a folded form.  In Molecular Chaperones: Methods and Protocols, expert researchers address a wide variety of approaches to the study these mechanisms, featuring the workings of heat shock proteins and heat shock transcription factors, in vitro and in vivo. Written in the highly successful Methods in Molecular Biology™ series format, chapters features 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, Molecular Chaperones: Methods and Protocols serves as an ideal guide for all scientists who wish to pursue this vital biological action and its impact on human health and disease.

Prince / Calderwood Molecular Chaperones jetzt bestellen!

Zielgruppe


Professional/practitioner

Weitere Infos & Material


Targeted Deletion of Hsf1, 2, and 4 Genes in Mice.- The Role Of Heat Shock Factors in Stress-Induced Transcription.- Hsp90 and Client Protein Maturation.- The Role of p23, Hop, Immunophilins, and Other Co-Chaperones in Regulating Hsp90 Function.- Detecting Hsp90 Phosphorylation.- Role of Molecular Chaperones in Biogenesis of the Protein Kinome.- Nucleotide Exchange Factors for Hsp70 Chaperones.- Reconstitution of CHIP E3 Ubiquitin Ligase Activity.- Structure-Functions of HspB1 (Hsp27).- Combined Lentiviral and RNAi Technologies for the Delivery and Permanently Silencing of the hsp25 Gene.- Quantification of HSP27 and HSP70 Molecular Chaperone Activities.- Measuring Hsp72 (HSPA1A) by Indirect Sandwich ELISA.- Analysis of Heat Shock Protein Localization Using Flow Cytometry.- Quantitation of Heat Shock Proteins in Clinical Samples Using Mass Spectrometry.- Bioinformatic Approach to Identify Chaperone Pathway Relationship from Large-Scale Interaction Networks.- Hsp70: Anti-Apoptotic and Tumorigenic Protein.- Determination of Cell Survival or Death.- Immunohistochemistry of Human Hsp60 in Health and Disease: From Autoimmunity to Cancer.- Preparation of a Heat Shock Proteins 70-Based Vaccine from DC-Tumor Fusion Cells.- Isolation of Heat Shock Protein Complexes.- Enhancing Antigen Cross-Presentation and T-Cell Priming by Complexing Protein Antigen to Recombinant Large Heat Shock Protein.- Investigating Receptors for Extracellular Heat Shock Proteins.- Analysis of Cellular Migration Using a Two-Chamber Methodology.



Ihre Fragen, Wünsche oder Anmerkungen
Vorname*
Nachname*
Ihre E-Mail-Adresse*
Kundennr.
Ihre Nachricht*
Lediglich mit * gekennzeichnete Felder sind Pflichtfelder.
Wenn Sie die im Kontaktformular eingegebenen Daten durch Klick auf den nachfolgenden Button übersenden, erklären Sie sich damit einverstanden, dass wir Ihr Angaben für die Beantwortung Ihrer Anfrage verwenden. Selbstverständlich werden Ihre Daten vertraulich behandelt und nicht an Dritte weitergegeben. Sie können der Verwendung Ihrer Daten jederzeit widersprechen. Das Datenhandling bei Sack Fachmedien erklären wir Ihnen in unserer Datenschutzerklärung.