Identification of Protein Interactions by Far Western Analysis

Far western blotting is a method of identifying protein‐protein interactions. One protein of interest is immobilized on a solid support membrane, then probed with a non‐antibody protein. Far western blots can be used to identify specific interacting proteins in a complex mixture of proteins. They are particularly useful for examining interactions between proteins that are difficult to analyze by other methods due to solubility problems or because they are difficult to express in cells. This method is performed totally in vitro, and the proteins of interest can be prepared in a variety of ways.

[1]  S. Stifani,et al.  The Groucho/Transducin-like Enhancer of split Transcriptional Repressors Interact with the Genetically Defined Amino-terminal Silencing Domain of Histone H3* , 1997, The Journal of Biological Chemistry.

[2]  E. Kremmer,et al.  Immunological detection of proteins associated with the Epstein-Barr virus nuclear antigen 2A. , 1993, Virology.

[3]  S. Kimball,et al.  Identification of Interprotein Interactions between the Subunits of Eukaryotic Initiation Factors eIF2 and eIF2B* , 1998, The Journal of Biological Chemistry.

[4]  A. Seiter,et al.  Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis. , 1988, The EMBO journal.

[5]  S. Spiess,et al.  Ligand Blot Analysis of Insulin-Like Growth Factor-Binding Proteins using Biotinylated Insulin-Like Growth Factor-I , 1997, Hormone Research in Paediatrics.

[6]  E. Fuchs,et al.  Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins , 1994, The Journal of cell biology.

[7]  E. Kremmer,et al.  Epstein-Barr Virus Nuclear Antigen 1 Forms a Complex with the Nuclear Transporter Karyopherin α2* , 1997, The Journal of Biological Chemistry.

[8]  A. Cupp,et al.  Role of basic-helix-loop-helix transcription factors in Sertoli cell differentiation: identification of an E-box response element in the transferrin promoter. , 1997, Endocrinology.

[9]  T. Schumacher,et al.  In Vitro Radiolabeling of Peptides and Proteins , 1995, Current protocols in protein science.

[10]  Chawnshang Chang,et al.  Isolation and Characterization of ARA160 as the First Androgen Receptor N-terminal-associated Coactivator in Human Prostate Cells* , 1999, The Journal of Biological Chemistry.

[11]  D. Edmondson,et al.  Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4. , 1996, Genes & development.

[12]  E. J. Luna,et al.  Biotinylation of Proteins in Solution and on Cell Surfaces , 1996, Current protocols in protein science.