Promega Corporation

Wisconsin Alumni Research Foundation

Brock Binkowski

Keith V Wood

Lance P Encell

Matthew B Robers

Monika G Wood

Mary P Hall

Thomas Machleidt

Thomas A Kirkland

Melanie Dart

Poncho Meisenheimer

James Unch

Said A Goueli

Nidhi Nath

Andrew S Dixon

Hicham Zegzouti

Marie Schwinn

Subhanjan Mondal

Dileep K Pulukkunat

Gediminas Vidugiris

Paul Otto

Michael R Slater

Frank Fan

Susan Wigdal

Braeden L Butler

Kristopher Zimmerman

Brad Hook

Ce Shi

Michael P Valley

Wenhui Zhou

James J Cali

Christopher Todd Eggers

Kris Zimmerman

Mei Cong

Pete Stecha

Dieter Klaubert

Hui Wang

Joel R Walker

Franco Cerrina

Andrew L Niles

Michael Richard Sussman

Peter Jeremy Belshaw

Kathryn E Richmond

James Howard Kaysen

Kevin Kupcho

Kimberly Risma

Braeden Butler

An isolated polynucleotide encoding a modified luciferase polypeptide and substrates. The OgLuc variant polypeptide has at least 60% amino acid sequence identity to SEQ ID NO: 1 and at least one amino acid substitution at a position corresponding to an amino acid in SEQ ID NO: 1. The OgLuc variant polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the corresponding polypeptide of the wild-typeluciferase.

-derived luciferases, novel coelenterazine substrates, and methods of use

Provided herein are compositions and methods for the assembly of a bioluminescent complex from two or more non-luminescent (e.g., substantially non-luminescent) peptide and/or polypeptide units. In particular, bioluminescent activity is conferred upon a non-luminescent polypeptide via structural complementation with another, complementary non-luminescent peptide.

Activation of bioluminescence by structural complementation

An isolated polynucleotide encoding a modified luciferase polypeptide and substrates. The OgLuc variant polypeptide has at least 60% amino acid sequence identity to SEQ ID NO: 1 and at least one amino acid substitution at a position corresponding to an amino acid in SEQ ID NO: 1. The OgLuc variant polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the corresponding polypeptide of the wild-type

Oplophorus-derived luciferases, novel coelenterazine substrates, and methods of use

Provided herein are systems and methods for characterizing target/ligand engagement. In particular, luciferase-labeled polypeptide targets are used to detect or quantify target/ligand engagement (e.g., within a cell or cell lysate).

Luciferase-based thermal shift assays

Compounds that may inhibit-derived luciferases are disclosed as well as compositions and kits comprising the compounds and methods of using the compounds.

Nanoluc suicide substrates

Activation of bioluminescene by structural complementation

Methods, kits and compositions containing a mixture of D-luciferin and L-luciferin for light generation with luciferase are disclosed that have improved stability when stored over time. The mixture of D-luciferin and L-luciferin can be used to detect the presence or amount of ATP or of luciferase in a sample.

Stabilized formulation for luminescent detection of luciferase and nucleoside phosphates

Described are pro-coelenterazine analogues, methods for making the analogues, kits comprising the analogues, and methods of using the compounds for the detection of luminescence in luciferase-based assays or fragment complementary luciferase. The disclosed pro-coelenterazine analogues provide increased serum stability for live cell assays, and are capable of tuning the brightness and assay windows as needed for the applications.

Serum stable pro-coelenterazine analogues

Growing community of inventors

Sauk City, WI, United States of America

Brock Binkowski