Promega Corporation

Other

Melanie Dart

Keith V Wood

Lance P Encell

Thomas A Kirkland

Thomas Machleidt

Brock Binkowski

Matthew B Robers

Mary P Hall

Nidhi Nath

Monika G Wood

Poncho Meisenheimer

Said A Goueli

James Unch

Andrew S Dixon

Hicham Zegzouti

Marie Schwinn

Subhanjan Mondal

Dileep K Pulukkunat

Ce Shi

Hui Wang

Wenhui Zhou

Michael Killoran

Virginia E Kincaid

Trish Hoang

Thomas P Smith

Rod Flemming

Becky Godat

Virginia Kincaid

Brock F Binkowski

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

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 compositions and methods for stabilizing coelenterazine and analogs or derivatives thereof, and for improving the solubility and reconstitution efficiency of coelenterazine and analogs and derivatives thereof.

Compositions and methods for stabilizing coelenterazine and analogs and derivatives thereof

Activation of bioluminescene by structural complementation

Provided herein are sulfo n-hydroxysuccimidyl ester (sulfo-SE) linked peptides, methods of synthesis thereof, and methods of using such peptides for labeling of biomolecules. In particular, peptides comprising non-alkyl group such as serine, threonine, cysteine, tyrosine, glutamic acid, and aspartic acid are stably modified (e.g., without autoreactivity) with a sulfo-SE group and used to label or otherwise modify biomolecules.

Reactive peptide labeling

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Madison, WI, United States of America

Melanie Dart