The purpose of this core unit is to provide the different project with oligonucleotides, synthetic peptides and purified recombinant proteins expressed in E. coli or in insect cells using the baculovirus expression system. The oligonucleotides will be used as linkers, PCR primers, probes for DNA binding assays, antisense inhibitors of gene expression and affinity ligands for the purification of DNA binding proteins. The peptides will be used as immunogens for preparation of anti-peptide antibodies, substrates for phosphorylation reactions, pseudosubstrate inhibitors of specific protein kinases and possibly phosphatases, ligands for protein purification and studying protein-protein interactions. Various transcription factors, such as cJun, T3Ralpha and E2A-Pbx1 and dominant acting inhibitors of them will be produced either in E. coli or in insect cells, purified and supplied to the various projects for microinjection experiments to study phosphorylation/dephosphorylation and interaction with other proteins. We will also produce various oncoproteins and kinases, such as Ha-Ras, vAb1, Erk1 and Erk2 to be used in microinjection experiments. This core will relieve the individual units from the routine chores of oligonucleotide, peptide and protein purification.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
5P01CA050528-07S2
Application #
6237093
Study Section
Project Start
1996-02-01
Project End
1998-01-31
Budget Start
1996-10-01
Budget End
1997-09-30
Support Year
7
Fiscal Year
1997
Total Cost
Indirect Cost
Name
University of California San Diego
Department
Type
DUNS #
077758407
City
La Jolla
State
CA
Country
United States
Zip Code
92093
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White, F C; Benehacene, A; Scheele, J S et al. (1997) VEGF mRNA is stabilized by ras and tyrosine kinase oncogenes, as well as by UV radiation--evidence for divergent stabilization pathways. Growth Factors 14:199-212
Knoepfler, P S; Kamps, M P (1997) The highest affinity DNA element bound by Pbx complexes in t(1;19) leukemic cells fails to mediate cooperative DNA-binding or cooperative transactivation by E2a-Pbx1 and class I Hox proteins - evidence for selective targetting of E2a-Pbx1 to a subset of P Oncogene 14:2521-31

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