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Laboratory methods in enzymology. Protein, Part D /

In this volume we have brought together a number of core protocols concentrating on Protein, carefully written and edited by experts.

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Lorsch, Jon (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: London : Elsevier Academic Press, 2015.
Edición:First edition.
Colección:Methods in enzymology ; v. 559.
Temas:
Acceso en línea:Texto completo
Texto completo

MARC

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245 0 0 |a Laboratory methods in enzymology.  |p Protein,  |n Part D /  |c edited by Jon R. Lorsch. 
250 |a First edition. 
264 1 |a London :  |b Elsevier Academic Press,  |c 2015. 
264 4 |c �2015 
300 |a 1 online resource (xviii, 470 pages) :  |b color illustrations 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
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490 1 |a Methods in Enzymology,  |x 0076-6879 ;  |v volume. 559 
504 |a Includes bibliographical references and index. 
505 0 0 |t Purification of His-tagged proteins --  |t Affinity purification of a recombinant protein expressed as a fusion with the maltose-binding protein (MBP) tag --  |t Immunoaffinity purification of proteins --  |t Affinity purification of protein complexes using TAP tags --  |t Strep-tagged protein purification --  |t Proteoloytic affinity tag cleavage --  |t Affinity pull-down of proteins using anti-FLAG M2 agarose beads --  |t Protein affinity prufication using intein-chitin binding protein tags --  |t Purification of GST-tagged proteins. 
505 0 |a Front Cover; Laboratory Methods in Enzymology: Protein Part D; Copyright; Contents; Contributors; Preface; Chapter One: Purification of His-Tagged Proteins; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions & buffers; 4. Protocol; 4.1. Preparation; 4.2. Duration; 5. Protocol A: Purification of His-tagged Proteins Under Native Conditions; 5.1. Tip; 6. Step 1A Preparation of a Cleared E. coli Lysate Under Native Conditions; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip; 6.5. Tip; 6.6. Tip; 6.7. Tip; 7. Step 2A Batch Purification of His-tagged Proteins from E. coli Under Native Conditions. 
505 8 |a 7.1. Overview7.2. Duration; 7.3. Tip; 7.4. Tip; 7.5. Tip; 7.6. Tip; 8. Step 1B Preparation of a Cleared E. coli Lysate Under Denaturing Conditions; 8.1. Overview; 8.2. Duration; 8.3. Tip; 8.4. Tip; 8.5. Tip; 8.6. Tip; 8.7. Tip; 9. Step 2B Batch Purification of His-tagged Proteins from E. coli Under Denaturing Conditions; 9.1. Overview; 9.2. Duration; 9.3. Tip; 9.4. Tip; 9.5. Tip; 9.6. Tip; References; Referenced Literature; Source References; Referenced Protocols in Methods Navigator. 
505 8 |a Chapter Two: Affinity Purification of a Recombinant Protein Expressed as a Fusion with the Maltose-Binding Protein (MBP) Tag1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions & buffers; 4. Protocol; 4.1. Duration; 4.2. Preparation; 5. Step 1 Equilibration of the Column; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 6. Step 2 Binding of the Protein Sample; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip; 7. Step 3 Removal of Unbound Proteins; 7.1. Overview; 7.2. Duration; 8. Step 4 Elution of the Bound Protein; 8.1. Overview; 8.2. Duration; 8.3. Tip; 8.4. Tip; 8.5. Tip; 8.6. Tip. 
505 8 |a 8.7. Tip8.8. Tip; References; Referenced Literature; Referenced Protocols in Methods Navigator; Chapter Three: Immunoaffinity Purification of Proteins; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions & buffers; 4. Protocol; 4.1. Duration; 4.2. Preparation; 4.3. Tip; 4.4. Tip; 5. Step 1 Equilibrate Column; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 6. Step 2 Loading the Column; 6.1. Overview; 6.2. Duration; 6.3. Tip; 7. Step 3 Washing the Column; 7.1. Overview; 7.2. Duration; 7.3. Tip; 8. Step 4 Elution of the Protein from the Column; 8.1. Overview; 8.2. Duration; 8.3. Tip. 
505 8 |a 8.4. Tip8.5. Tip; 8.6. Tip; 9. Step 5 Column Regeneration and Storage; 9.1. Overview; 9.2. Duration; 9.3. Tip; References; Referenced Protocols in Methods Navigator; Chapter Four: Affinity Purification of Protein Complexes Using TAP Tags; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions & buffers; 4. Protocol; 4.1. Preparation; 4.2. Duration; 5. Step 1 Preparation of Protein Lysates; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip; 6. Step 2 Binding of the Protein A Tag to IgG-Sepharose; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip; 6.5. Tip; 6.6. Tip 7 Step 3 TEV Protease Cleave. 
588 0 |a Print version record. 
520 |a In this volume we have brought together a number of core protocols concentrating on Protein, carefully written and edited by experts. 
650 0 |a Proteins  |x Analysis. 
650 6 |a Prot�eines  |x Analyse.  |0 (CaQQLa)201-0031951 
650 7 |a SCIENCE  |x Life Sciences  |x Biochemistry.  |2 bisacsh 
650 7 |a Proteins  |x Analysis  |2 fast  |0 (OCoLC)fst01079714 
650 7 |a Proteins  |x Purification  |2 fast  |0 (OCoLC)fst01079750 
700 1 |a Lorsch, Jon,  |e editor. 
776 0 8 |i Print version:  |a Lorsch, Jon.  |t Laboratory Methods in Enzymology: Protein Part D.  |d Burlington : Elsevier Science, �2015  |z 9780128002797 
830 0 |a Methods in enzymology ;  |v v. 559.  |x 0076-6879 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/559  |z Texto completo 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/book/9780128002797  |z Texto completo