Insoluble Proteins [E-Book] : Methods and Protocols / edited by Elena Garcia Fruitós, Anna Arís Giralt
This volume serves to aid researchers working in the recombinant protein production field by describing a wide number of protocols and examples. Chapters describe recombinant protein production in different expression systems, prokaryotic and eukaryotic expression systems, purification protocols, ch...
Saved in:
Full text |
|
Personal Name(s): | Aris Giralt, Anna, editor |
Garcia Fruitos, Elena, editor | |
Edition: |
2nd edition 2022. |
Imprint: |
New York, NY :
Humana Press,
2022
|
Physical Description: |
XVI, 533 pages 98 illustrations, 60 illustrations in color (online resource) |
Note: |
englisch |
ISBN: |
9781071618592 |
DOI: |
10.1007/978-1-0716-1859-2 |
Series Title: |
/* Depending on the record driver, $field may either be an array with
"name" and "number" keys or a flat string containing only the series
name. We should account for both cases to maximize compatibility. */?>
Methods in Molecular Biology ;
2406 |
Subject (LOC): |
- General Introduction: Recombinant protein production and purification of insoluble proteins
- Overcoming the solubility problem in E. coli: available approaches for recombinant protein production
- A3D 2.0 update for the prediction and optimization of protein solubility
- Tailoring codon usage to the underlying biology for protein expression optimization
- Protein Expression Optimization Strategies in E. coli: A Tailored Approach in Strain Selection and Parallelizing Expression Conditions
- A novel approach for production of aggregation prone proteins using the spidroin-derived NT* tag
- Cleavable Self-Aggregating Tags (cSAT) for Therapeutic Peptide Expression and Purification
- Use Intein Cleavable Polyhydroxyalkanoate Synthase Fusions to Improve Protein Solubility
- Introduction of a hexalysine (6K) tag can protect from N-terminal cleavage and increase yield of recombinant proteins expressed in the periplasm of E. coli
- Two-tiered selection and screening strategy to increase functional enzyme production in Escherichia coli
- Method for production of cysteine-rich proteins in Lactococcus lactis expression system
- Heterologous protein production in Lactobacillus (plantarum) using pSIP vectors
- Soluble recombinant protein production in Pseudoaltermonas haloplanktis TAC125: the case study of the full-length human CDKL5 protein
- A protocol to enhance soluble protein expression in the cytoplasm of Bacillus subtilis
- Applications of cell-free synthesized membrane protein precipitates
- High cell-density expression system: yeast cells in a phalanx efficiently produce a certain range of "difficult-to-express" secretory recombinant proteins
- Insect Cells-Baculovirus system for the production of difficult to express proteins: from expression screening for soluble constructs to protein quality control
- Transient gene expression in human Expi293 cells
- Recombinant Expression of Complex Proteins in Human Cells Lines
- Optimizing chaperone removal strategy from over-expressed recombinant proteins: GNE, a case study
- Intrinsically disordered proteins (IDP): purification under denaturing conditions
- Solubilization and Refolding of Inclusion Body Proteins
- Non-denaturing solubilization of Inclusion Bodies from Lactic Acid Bacteria
- Purification of Inclusion Bodies Produced in Bacteria and Yeast
- Eukaryotic aggresomes: protocols and tips for their production, purification and handling
- Characterization of the conformational properties of soluble and insoluble proteins by Fourier transform infrared spectroscopy
- Characterizing Soluble Protein Aggregates using Native Mass Spectrometry Coupled with Temperature-control Electrospray Ionization and Size-exclusion Chromatography
- Quality control of proteins solubilized from inclusion bodies
- Methods for the Characterization of Protein Aggregates
- Insoluble Protein Applications: The Use of Bacterial Inclusion Bodies as Biocatalysts
- Methods for Processing Protein Aggregates into Surfaces. .