Abstract: The invention features computer-assisted methods for identifying molecules which will bind to the EPO receptor and act as an erythropoietin (EPO) mimetic. Preferred EPO mimetics identified using the method of the invention act as agonists of the EPO receptor in one or more in vitro or in vivo biological assays of EPO activity.

Abstract: The invention features computer-assisted methods for identifying molecules which will bind to the EPO receptor and act as an erythropoietin (EPO) mimetic. Preferred EPO mimetics identified using the method of the invention act as agonists of the EPO receptor in one or more in vitro or in vivo biological assays of EPO activity.

Abstract: The invention features computer-assisted methods for identifying molecules which will bind to the EPO receptor and act as an erythropoietin (EPO) mimetic. Preferred EPO mimetics identified using the method of the invention act as agonists of the EPO receptor in one or more in vitro or in vivo biological assays of EPO activity.

Abstract: The present invention provides a new subcutaneous injection dosing regimen for erythropoietin to treat anemia. The new erythropoietin treatment regimen of the present invention results in improved hemoglobin levels with less frequent dosing.

Abstract: The binding specificity of the murine OKT3 has been transferred into a human antibody framework in order to reduce its immunogenicity. “Humanized” anti-CD3 mAbs, such as gOKT3-5 and gOKT3-7, have been shown to retain, in vitro, all the properties of native OKT3, including T cell activation which has been correlated, in vivo, with the severe side-effects observed in transplant recipients after the first administration of the mAb. Disclosed are modified versions of humanized anti-CD3 mAbs that do not have the property of T cell activation. Further dislosed are methods of using such mAbs.

Abstract: The binding specificity of the murine OKT3 has been transferred into a human antibody framework in order to reduce its immunogenicity. These “humanized” anti-CD3 monoclonal antibodies retain, in vitro, all the properties of native anti-CD3 antibodies, including T cell activation which has been correlated, in vivo, with the severe side-effects observed in transplant recipients after the first administration of the mAb.

Abstract: There are disclosed: a CDR-grafted antibody having at least one chain wherein the framework regions are predominantly derived from a first antibody (acceptor) and at least one CDR is derived from a second antibody (donor), the CDR-grafted antibody being capable of binding to the CD4 antigen; processes for its production; nucleotide sequences for use in its production; compositions containing

Abstract: The extracellular domain of the human erythropoietin receptor (EPO binding protein, EBP) has been expressed and overproduced in E. coli. Control of oxygen levels and pH during high density fermentation allows the production of only the protein variant with the native amino terminus. Methods disclosed permit the efficient recovery of purified EBP which quantitatively binds EPO. The active purified protein competes with membrane associated EPO receptor for binding [125I]EPO and neutralizes EPO dependent stimulation in a cell based proliferation assay. Further, the radioligand equilibrium binding constant for this interaction has been determined by immobilizing EBP on agarose gel via a free cysteine. The EBP of the present invention has many uses including the structural determination of the protein by NMR or crystallography, in drug design and discovery, and as a therapeutic. A fusion protein of EBP and an immunoglobulin heavy chain was also produced.

Abstract: The binding specificity of the murine OKT3 has been transferred into a human antibody framework in order to reduce its immunogenicity. This "humanized" anti-CD3 mAb (gOKT3-5) was previously shown to retain, in vitro, all the properties of native OKT3, including T cell activation which has been correlated, in vivo, with the severe side-effects observed in transplant recipients after the first administration of the mAb. Disclosed is a single amino acid mutation from a leucine to a glutamic acid at position 235 in the Fc receptor (FcR) binding segment of the gOKT3-5 mAb to produce Glu-235 mAb. Also disclosed is an amino acid mutation from the contiguous phenylalanine at position 234 to a leucine (Leu-234).

Abstract: The invention features computer-assisted methods for identifying molecules which will bind to the EPO receptor and act as an erythropoietin (EPO) mimetic. Preferred EPO mimetics identified using the method of the invention act as agonists of the EPO receptor in one or more in vitro or in vivo biological assays of EPO activity.

Abstract: Peptides of 10 to 40 or more amino acid residues in length and having the sequence X.sub.3 X.sub.4 X.sub.5 GPX.sub.6 TWX.sub.7 X.sub.8 (SEQ ID NO:252) where each amino acid is indicated by standard one letter abbreviation; X.sub.3 is C; X.sub.4 is R, H, L, or W; X.sub.5 is M, F, or I; X.sub.6 is independently selected from any one of the 20 genetically coded L-amino acids; X.sub.7 is D, E, I, L, or V; and X.sub.8 is C, which bind and activate the erythropoietin receptor (EPO-R) or otherwise act as an EPO agonist, and methods for their use.