Generation of cDNA Libraries : Methods and Protocols /
Corporate Author: | |
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Other Authors: | |
Format: | eBook |
Language: | English |
Published: |
Totowa, NJ :
Humana Press : Imprint: Humana,
2003.
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Edition: | 1st ed. 2003. |
Series: | Methods in Molecular Biology,
221 |
Subjects: |
Table of Contents:
- Complementary DNA Libraries
- Rapid Amplification of cDNA Ends
- cDNA Generation on Paramagnetic Beads
- Construction of a Normalized cDNA Library by mRN-cDNA Hybridization and Subtraction
- Amplification of cDNA Ends Using PCR Suppression Effect and Step-Out PCR
- Use of Inverse PCR to Clone cDNA Ends
- Construction of Size-Fractionated cDNA Library Assisted by an In Vitro Recombination Reaction
- Construction of a Full-Length Enriched and a 5?-End Enriched cDNA Library Using the Oligo-Capping Method
- cDNA Library Construction Using In Vitro Transcriptional Amplification
- Amplification of Representative cDNA Pools from Microscopic Amounts of Animal Tissue
- Single-Cell cDNA Library Construction Using Cycling aRNA Amplification
- mRNA/cDNA Library Construction Using RNA-Polymerase Cycling Reaction
- Quality Assessment of cDNA Libraries
- Assessment of the Quality of mRNA Libraries by Agarose Gel Electrophoresis
- PACS RT-PCR
- Single-Cell mRNA Library Analysis by Northern Blot Hybridization
- Generation of cDNA Libraries for Profiling Gene Expression of Given Tissues or Cells
- Screening Poly [dA/dT(?)] cDNA for Gene Identification
- Generation of Longer cDNA Fragments from SAGE Tags for Gene Identification
- Generation of Full-Length cDNA Libraries Enriched for Differentially Expressed Genes
- Subtractive Hybridization for the Identification of Differentially Expressed Genes Using Uraci-DNA Glycosylase and Mung-Bean Nuclease
- Subtractive Cloning of Differential Genes Using RNA-PCR
- Strategy for Construction of a cDNA Encoding a Repetitive Amino Acid Sequence
- Preparing Lambda Libraries for Expression of Proteins in Prokaryotes or Eukaryotes
- Peptide Library Construction from RNA-PCR-Derived RNAs
- Identifying Interacting Proteins in an Escherichia coli-Based Two-Hybrid System
- Future Perspectives.