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The Resource Laboratory methods in enzymology, Part D, Protein, edited by Jon R. Lorsch

Laboratory methods in enzymology, Part D, Protein, edited by Jon R. Lorsch

Label
Laboratory methods in enzymology, Part D, Protein
Title
Laboratory methods in enzymology
Title number
Part D
Title part
Protein
Statement of responsibility
edited by Jon R. Lorsch
Contributor
Editor
Subject
Genre
Language
eng
Summary
In this volume we have brought together a number of core protocols concentrating on Protein, carefully written and edited by experts
Member of
Cataloging source
EBLCP
Dewey number
572/.6
Illustrations
illustrations
Index
index present
LC call number
QP601
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
Lorsch, Jon
Series statement
Methods in Enzymology,
Series volume
volume. 559
http://library.link/vocab/subjectName
  • Proteins
  • SCIENCE
  • Proteins
  • Proteins
Label
Laboratory methods in enzymology, Part D, Protein, edited by Jon R. Lorsch
Instantiates
Publication
Copyright
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Carrier MARC source
rdacarrier
Content category
text
Content type code
  • txt
Content type MARC source
rdacontent
Contents
  • Purification of GST-tagged proteins
  • Purification of His-tagged proteins
  • Affinity purification of a recombinant protein expressed as a fusion with the maltose-binding protein (MBP) tag
  • Immunoaffinity purification of proteins
  • Affinity purification of protein complexes using TAP tags
  • Strep-tagged protein purification
  • Proteoloytic affinity tag cleavage
  • Affinity pull-down of proteins using anti-FLAG M2 agarose beads
  • Protein affinity prufication using intein-chitin binding protein tags
  • 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
  • 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
  • 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
  • 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
  • 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
Control code
914434179
Edition
First edition.
Extent
1 online resource (xviii, 470 pages)
Form of item
online
Isbn
9780128003350
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
Other physical details
color illustrations.
Specific material designation
remote
System control number
(OCoLC)914434179
Label
Laboratory methods in enzymology, Part D, Protein, edited by Jon R. Lorsch
Publication
Copyright
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Carrier MARC source
rdacarrier
Content category
text
Content type code
  • txt
Content type MARC source
rdacontent
Contents
  • Purification of GST-tagged proteins
  • Purification of His-tagged proteins
  • Affinity purification of a recombinant protein expressed as a fusion with the maltose-binding protein (MBP) tag
  • Immunoaffinity purification of proteins
  • Affinity purification of protein complexes using TAP tags
  • Strep-tagged protein purification
  • Proteoloytic affinity tag cleavage
  • Affinity pull-down of proteins using anti-FLAG M2 agarose beads
  • Protein affinity prufication using intein-chitin binding protein tags
  • 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
  • 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
  • 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
  • 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
  • 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
Control code
914434179
Edition
First edition.
Extent
1 online resource (xviii, 470 pages)
Form of item
online
Isbn
9780128003350
Media category
computer
Media MARC source
rdamedia
Media type code
  • c
Other physical details
color illustrations.
Specific material designation
remote
System control number
(OCoLC)914434179

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