Promega Corporation

Danisco US Inc.

Lance P Encell

Keith V Wood

Monika G Wood

Mary P Hall

Brock Binkowski

Matthew B Robers

Thomas A Kirkland

Gediminas Vidugiris

Paul Otto

Aldis Darzins

Thomas Machleidt

Poncho Meisenheimer

Melanie Dart

Dieter Klaubert

Chad Zimprich

Georgyi V Los

Michael R Slater

Andrew S Dixon

Marie Schwinn

Kristopher Zimmerman

Mark McDougall

James Unch

Said A Goueli

Nidhi Nath

Hicham Zegzouti

Subhanjan Mondal

Dileep K Pulukkunat

Ce Shi

Kris Zimmerman

Rachel Friedman Ohana

Frank Fan

Braeden L Butler

Susan Wigdal

Kate Qin Zhao

Brad Hook

Tonny Johnson

Michael Killoran

Pete Stecha

Volker Schellenberger

Wenhui Zhou

Michael P Valley

Thomas B Morrison

Trish Hoang

Kimberly Risma

Beat O Blattmann

John M Davis

Gregory T Mrachko

Virginia Kincaid

Brock F Binkowski

Braeden Butler

Chad Zimbrich

Aldis Darzin

Provided herein are isolated polynucleotide encoding modified click beetle luciferase polypeptides that have enhanced luminescence and longer wavelength near-infrared signals. The disclosure also relates to near-infrared bioluminescence systems that include said modified click beetle luciferase polypeptides and novel luciferin derivatives, as well as methods of using said modified click beetle luciferase polypeptides and bioluminescence systems.

Luciferase sequences utilizing infrared-emitting substrates to produce enhanced luminescence

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

Provided herein are bioluminescent polypeptides and compositions and methods for the assembly of a tripartite or multipartite bioluminescent complex. In particular embodiments, a bioluminescent complex is formed upon the interaction of three or more peptide and/or polypeptide components.

Multipartite luciferase peptides and polypeptides

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

Provided herein are enhanced luciferase enzymes for use with thermostable luciferin analogs for bioluminescent assays. In particular, the present disclosure provides compositions, assays, and methods for performing a bioluminescent assay using enhanced, high-activity luciferase enzymes compatible with thermostable luciferins, such as 5,5-disubstituted luciferin analogs.

Luciferase enzymes for use with thermostable luciferins in bioluminescent assays

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

Syntheticluciferases with enhanced light output

Activation of bioluminescene by structural complementation

Provided herein are substantially non-luminescent peptide/polypeptide tags that are inserted internally within a protein of interest or between N-terminal and C-terminal peptides/polypeptides. Interaction of the internally-inserted tag with a complement polypeptide/peptide that is also substantially non-luminescent results in the formation a bioluminescent reporter complex.

Internal protein tags

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

Synthetic oplophorus luciferases with enhanced light output

Growing community of inventors

Fitchburg, WI, United States of America

Lance P Encell