Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Gail F. Seelig"'
Publikováno v:
Journal of Biological Chemistry. 269:5548-5553
A synthetic segment (110-127) of the carboxyl terminus of recombinant human granulocyte-macrophage colony-stimulating factor (rh-GM-CSF) was used to generate a rabbit polyclonal antibody (345-6), which recognized both peptide and full-length Escheric
Publikováno v:
Journal of Biological Chemistry. 269:358-363
The epitopes of two neutralizing antibodies (47N3-6 and 47N30A35) raised against rhuIFN-gamma each mapped both to amino-terminal regions (22-29 and 12-19, respectively) and to a carboxyl-terminal region 131-139, suggesting the juxtaposition of these
Autor:
Gail F. Seelig, Doreen Borkowski, William T. Windsor, Hung V. Le, Rosalinda Syto, Paul P. Trotta, Lata Ramanathan
Publikováno v:
Biochemistry. 30:9576-9582
Human interleukin 4 is a 129 amino acid lymphokine secreted by activated T cells that exerts pleiotropic biological effects on B and T lymphocytes and other hematopoietic cells. Structure-function relations were studied by employing selective proteol
Autor:
Yuzuru Kanakura, Christopher B. Brown, Gail F. Seelig, Kenneth Kaushansky, Stephen A. Cannistra, James D. Griffin, Winifred W. Prosise, Julio C. Hawkins, Masato Nakamura
Publikováno v:
Blood. 77:1033-1043
Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a glycoprotein that is required for the survival, growth, and differentiation of hematopoietic progenitor cells. Although the primary structure of GM-CSF is known from cDNA cloning, the rel
Autor:
Catherine Favre, Gail F. Seelig, Sylvie Benureau, Odile Neyret, Nicholas Lydon, Sylvie Bove, Alan M. Levine, Tatanahalli L. Nagabhushan, Paul P. Trotta
Publikováno v:
Biochemistry. 24:4131-4141
A panel of five monoclonal antibodies, designated U1-U5, produced by murine hybridoma clones has been raised to recombinant interferon (IFN) alpha-2, and one monoclonal antibody, designated U6, has been raised to a mixture of cyanogen bromide fragmen
Autor:
Gail F. Seelig, J. E. Folk
Publikováno v:
Journal of Biological Chemistry. 255:9589-9593
The reactivities of human plasma factor XIIIa toward iodoacetic acid and toward alpha-bromo-4-hydroxy-3-nitroacetophenone have been studied under conditions where this dimeric enzyme reacts with the reagents in half-of-the-sites fashion and under con
Publikováno v:
Biochemistry. 27(6)
A panel of 18 murine monoclonal antibodies was raised in BALB/c mice to the full-length, 146 amino acid residue recombinant human gamma interferon (rHuIFN gamma-A). Two monoclonal antibodies, designated 47N3-6 and 30N47-1, were purified from ascites