Igen International, Inc.

Other

Cambridge Isotope Laboratories, Inc.

Proteinix Corporation

Richard C Titmas

Richard J Massey

Mark T Martin

Michael Joseph Powell

Andrew D Napper

John H Kenten

Rodger G Smith

Wonpyo Hong

Richard O Williams

Reid W Von Borstel

Balreddy Kamireddy

David M Simpson

Jan M Casadei

George B Sigal

John Gerald McCafferty

David John Chiswell

Liwen Dong

Michael J Darsley

William Wakefield Wood

Marwan ElMasri

Howie Tjiong

Salim Barkallah

Steven Michael Torkelson

Md Athar Masood

William James Ryan

Paul M Booth

Anthony R Rees

Mark Donald Schwinden

Joel Chandler Bradley

Janusz Konrad Kozak

Kevin Fitzgerald

Athar Masood

This invention relates to lysine isotopologues of Formulas I and 1-A, as described herein, and processes for synthesizing the same and derivatives and intermediates involved therein. In one aspect, described herein is a chemical compound comprising an isotopically labeled analog, i.e., an isotopologue of a standard or naturally occurring lysine. The lysine isotopologue is synthetically formed to have stable isotopes of elements incorporated at selected positions. As such, the lysine isotopologue has a molecular mass different from the mass of a standard or naturally occurring lysine.

Lysine isotopologues, compositions comprising the same and methods of synthesis

Antigens capable of eliciting antibodies which can catalyze chemical reactions, in particular, the cleavage or formation of a peptide linkage, comprising a hapten or a hapten and a suitable carrier molecule are disclosed. Haptens include, among others, silicon and boron containing compounds. Antibodies which are catalytically active for chemical reactions, in particular, the cleavage or formation of a selected peptide linkage or an ester bond, and which are elicited by such antigens are disclosed as well as methods for producing the antibodies and methods for catalyzing the cleavage or formation of a peptide linkage or in ester bond in a molecule.

Transition state analogs

Bipyridine or phenanthroline ligands presenting functional groups that prevent non-specific binding (in particular, negatively charged functional groups that are unaffected by standard conditions for conjugating biological reagents through amide bonds) are described as are luminescent metal complexes comprising these ligands. The use of luminescent ruthenium and osmium complexes comprising these ligands in electrochemiluminescence assays shows that the use of these labels can significantly reduce the amount of non-specific binding observed relative to assays carried out using reagents labeled with analogous labels that don't present functional groups that decrease non-specific binding.

ECL labels having improved non-specific binding properties, methods of using and kits containing the same

Catalytic antibodies are disclosed. The catalytic antibodies are specific for prodrug compounds. The catalytic antibodies enhance cleavage of an active drug moiety from a prodrug residue, thereby activating the drug.

Prodrugs activated by targeted catalytic proteins

Antigens capable of eliciting antibodies which can enhance the rate of chemical reactions at peptide bonds are disclosed. In particular, the rate of cleavage or formation of metastable peptide bonds, such as ASN-X, ASP-X, GLN-X, GLU-X, LYS-X, and HIS-Y-X, where X and Y are any amino acid, is enhanced by antibodies elicited by said antigen.

Methods for enhancing the rate of modification of metastable bonds

Catalytic antibodies which hydrolyze primary amides and methods for eliciting and use of such antibodies

Prodrugs that are activated by and conjugated to a catalytic antibody conjugated to a moiety that binds to a tumor cell population are provided.

A method for increasing the rate of a chemical reaction involving conversion of at least one reactant to at least one product which comprises contacting the reactant with at least one appropriate monoclonal antibody to the reactant under suitable conditions permitting formation of a complex between the monoclonal antibody and the reactant, conversion of the reactant to the product and release of the product from the complex, the monoclonal antibody being characterized by a K&gt;1, where K=k.sub.r /k.sub.p, k.sub.r is the affinity constant of the monoclonal antibody for the reactant and k.sub.p is the affinity constant of the monoclonal antibody for the product, by an r.sub.1 &gt;r.sub.0, where r.sub.1 is the rate of formation of the complex between the antibody and the reactant and where r.sub.0 is the rate of the chemical reaction in the absence of monclonal antibody, by an r.sub.2 &gt;r.sub.0, where r.sub.2 is the rate of the conversion of the complexed reactant to the complexed product and by an r.sub.3 &gt;r.sub.0, where r.sub.3 is the rate of release of the product from the complex.

Method of catalyzing stereochemical reactions

Catalytic antibodies which hydrolyze primary amides and methods for

Disclosed and claimed are methods for producing catalytic antibodies, including human catalytic antibodies, from bacteriophage. The methods require the cloning, selection, screening, and isolation of catalytic antibodies. Also disclosed and claimed are the products themselves, the catalytic antibodies, made from the phage technology. In addition, catalytic antibodies produced from the phage technology and useful in prodrug activation are disclosed and claimed. And finally, the invention also understands the production of catalytic antibodies to phosphonates.

Isolation and production of catalytic antibodies using phage technology

Growing community of inventors

Rockville, MD, United States of America

Richard C Titmas