Life Technologies Corporation

Bellbrook Labs, LLC

Karen Kleman-Leyer

Richard Somberg

Tony Klink

Jane A Beebe

David Lasky

Robert G Lowery

Matt Staeben

Thane Westermeyer

Elizabeth A Werner

Kurt William Vogel

Kevin Kupcho

Compositions, methods, and kits for detecting and monitoring kinase, phosphatase and protein post-translational modification activity are described. The compositions typically include a peptide, a detectable moiety, and a protease cleavage site. Modification of a peptide by a kinase, phosphatase or other protein post-translational modification alters the proteolytic sensitivity of the peptide, resulting in a change of a detectable property of the composition. Panel assays for determining substrates or modulators of kinase, phosphatase or other protein post-translational modification activity are also described.

Kinase and phosphatase assays

An isolated antibody produced against a donor product of an enzymatically catalyzed group transfer reaction is disclosed. In one aspect, the antibody has the ability to preferentially recognize the donor-product guanosine diphosphate (GDP), in the presence of the donor molecule guanosine triphosphate (GTP). Immunuoassays using compositions including such antibodies and kits for performing the immunoassays are also disclosed.

Assay method for group transfer reactions

The present invention relates to methods for detecting, quantifying and high throughput screening of donor-products and the catalytic activities generating the donor-products in group-transfer reactions. The invention further provides immunoassays, antibodies and kits that may be used to practice the methods of the invention.

Antibody that binds uridine diphosphate

Compositions, methods, and kits for detecting and monitoring post-translational modification activities, including kinase or phosphatase activities, are described. The compositions typically include a peptide, a first detectable moiety, a first binding member, and a protease cleavage site. Modification of a composition by a post-translational modification enzyme, such as a kinase or phosphatase, alters the proteolytic sensitivity of the peptide, resulting in a change of a detectable property of the composition when it is associated noncovalently with a probe composition that includes a second binding member and a second detectable moiety. Panel assays for determining substrates or modulators of enzymatic activities are also described.

Bimolecular optical probes

Compositions, methods, and kits for detecting and monitoring kinase or phosphatase activity are described. The compositions typically include a peptide, a detectable moiety, and a protease cleavage site. Modification of a peptide by a kinase or phosphatase alters the proteolytic sensitivity of the peptide, resulting in a change of a detectable property of the composition. Panel assays for determining substrates or modulators of kinase or phosphatase activity are also described.

The present invention relates to methods for detecting, quantifying and high throughput screening of donor-products and the catalytic activities generating the donor-products in group-transfer reactions catalyzed by adenosine triphosphatase (ATPase) or guanine triphosphatase (GTPase). The invention further provides immunoassays, antibodies and kits that may be used to practice the methods of the invention.

Growing community of inventors

Madison, WI, United States of America

Karen Kleman-Leyer