Jul. 21, 2025

PARP1/PARP2 is often overexpressed in various cancers, including breast, ovarian, prostate, lung, and glioblastoma. This overexpression is thought to support tumor cell survival. Some PARP inhibitors not only block the catalytic activity of PARP1/PARP2 but also trap PARP1/PARP2 on DNA at sites of damage, preventing its release. This creates a toxic DNA-protein complex that interferes with DNA replication and repair, leading to cell death, particularly in cancer cells deficient in homologous recombination repair (e.g., BRCA1/2-mutant cells).

Performance Characteristics:

May. 19, 2025

PD-1 and OX40 and corresponding ligands PD-L1 and OX40L, respectively, are attractive drug targets for immunotherapy. Aurora Biolabs has developed and manufactured TR-FRET assays for more than a decade. TR-FRET assays are know to be more sensitive than traditional enzyme-based assays due to the lanthanide-based donor fluorophores, which have long fluorescence lifetimes, and time-resolved detection, which minimizes background fluorescence interference.

Mar. 28, 2025

Aurora Biolabs, a recognized leader in RAS-targeted protein production, assay development, and co-crystal structure determination, has announced the launch of the industry’s first binding assay for screening KRAS G12D/Cyclophilin A (CypA)/inhibitor tri-complexes. This milestone represents a significant leap in accelerating drug discovery for one of the most critical oncogenic targets in cancer biology.

KRAS mutations—particularly G12D—are frequently implicated in lung, colon, and pancreatic cancers, locking RAS proteins in a constitutively active GTP-bound "ON" state. These mutant proteins drive unchecked cell proliferation and tumor growth by persistently activating downstream effector pathways. While RAS has long been considered "undruggable," the emergence of tri-complex inhibitors offers a transformative approach. Revolution Medicines has pioneered this field with macrocyclic compounds that first bind Cyclophilin A, then selectively engage RAS(ON) to form a tri-complex that sterically blocks effector interaction.

To support the development of this next generation of RAS(ON) inhibitors, Aurora Biolabs now offers a proprietary binding assay capable of quantifying the formation of the KRAS G12D/CypA/inhibitor tri-complex. This assay delivers rapid, reliable data essential for screening compound libraries and optimizing drug candidates targeting the oncogenic RAS state. It complements Aurora's extensive toolkit, including high-quality KRAS mutant proteins, assay kits, and structure determination services, forming a complete solution for RAS-targeted drug discovery.

“Our goal is to deliver the fastest and most accurate tools to support KRAS-targeted therapy development,” said Dr. May Zheng, the project manager of Aurora Biolabs. “By enabling researchers to directly assess tri-complex formation in vitro, we are bridging a critical gap in translational oncology and accelerating the path toward effective therapies for KRAS-driven cancers.”

Aurora Biolabs invites collaboration with biotech and pharmaceutical partners aiming to explore or expand their RAS inhibitor pipelines. With the introduction of this cutting-edge assay, the company solidifies its position at the forefront of RAS drug discovery support.

For more information, visit www.aurorabiolabs.com or contact the Aurora Biolabs team at info@aurorabiolabs.com.

Oct. 07, 2024

Affinity tags are highly effective tools used for the expression and purification of recombinant proteins. However, these tags are not meant to be permanent fixtures on their respective recombinant proteins. Therefore, removal of an affinity tag is essential for further structural and functional studies of a specific protein.

• PreScission Protease (HRV 3C Protease) (Ready to use)

• Recombinant SUMO Protease (ULP1) (Ready to use)

• TEV Protease (Ready to use)

Apr. 02, 2022

SARS-CoV-2, the viral agent responsible for the COVID-19 pandemic, is composed of an assortment of gene products critical to the viral lifecycle. We offer an assortment of SARS-CoV-2 recombinant proteins, kits, and services to advance your research and drug discovery needs.

• SARS-CoV-2 Main/3CL Protease

• SARS-CoV-2 Mpro Assay Kit

• Recombinant SARS-CoV-2 Papain-like Protease

• SARS-CoV-2 PLpro Assay Kit

• Recombinant SARS-CoV-2 Helicase

• Recombinant SARS-CoV-2 NSP7

• Recombinant SARS-CoV-2 NSP8

About SARS-CoV-2 Protease assays:

Our protease activity assays for our kits/service are FRET based assays. The assay kits are designed to detect the cleavage of peptide substrates specific for the protease of interest, either Mpro or PLpro, and is designed for inhibitor screening applications. In general, the assay is fast and convenient, and requires just two steps. In the first step, the protease enzyme is preincubated with inhibitor for 30 minutes. The reaction is initiated by adding protease substrate at the second step. Fluorescence intensity is measured with a fluorescent plate reader at the excitation wavelengths of 340-360 nm and emission wavelengths of 460-480 nm.

Mar. 01, 2022

The KRAS gene plays important roles in cell division, cell differentiation, and apoptosis. We offer an assortment of KRAS recombinant protein, kits, and services to advance your research and drug discovery needs.

• Kras wild-type and mutants (G12C, G12D, G12R, G12V) (apo)

• Kras wild-type and mutants (G12C, G12D, G12R, G12V) + GDP loaded

• Kras wild-type and mutants (G12C, G12D, G12R, G12V) + GppNHp loaded (for activity binding assay)

• Kras wild-type and mutants (G12C, G12D, G12R, G12V) TR-FRET based Nucleotide exchange assay kits

• Kras wild-type and mutants (G12C, G12D, G12R, G12V) TR-FRET based Kras -cRAF binding assay

• Kras assay services (Compound screening and profiling)

• Human recombinant SOS1 and cRAF

KRAS Nucleotide exchange assay

Our Nucleotide exchange assay for our kits/service is a TR-FRET based assay. The assay kit is designed to detect the GTP binding status of Kras in the presence of SOS1, a known Kras Guanine exchange factor. The Kras in our assay has a GST tag, that can bind to a Terbium-labeled anti-GST antibody (HTRF donor). If the Kras binds to a fluorescence-labeled GTP (HTRF acceptor), the donor and the acceptor will be brought in close proximity. Excitation of Terbium (340 nm) generates fluorescence resonance energy transfer (FRET) to fluorescence-labeled GTP acceptor, which emits specific fluorescence at 665 nm (figure below). Thus, GTP binding to the Kras can be quantitively measured by calculation of fluorescent ratio of 665 nm/620 nm.

Graphical Represntation of KRAS Nucleotide Exchange Assay Principle

Kras-cRAF binding assay

The Kras-cRAF binding assay is a TR-FRET based assay. In this assay, Kras is loaded with GppNHp, representing the activated Kras. The assay kit is designed to detect binding between Kras and cRAF. The Kras in this assay kit has a GST tag, that can bind to a Terbium-labeled anti-GST antibody (HTRF donor), and cRAF in this assay kit has a His tag, that can bind to a fluorescence-labeled anti-His antibody (HTRF acceptor). The binding of Kras with cRAF results in fluorescence resonance energy transfer (FRET) from the HTRF donor to the HTRF acceptor when the donor is activated allowing cRAF binding to be measured.

Graphical Represntation of Kras-cRAF Binding Assay Principle

Feb. 03, 2015

Aurora Biolabs, Inc. (ABL) is excited to announce that we are starting to offer highly purified eIF4E proteins for research and drug discovery.

Control of mRNA translation plays a critical role in cell growth, proliferation, differentiation, and anti-cancer drug discovery. A key player in the regulation of this process is the mRNA 5′ cap-binding protein, eukaryotic translation initiation factor 4E (eIF4E). Human EIF4E is a eukaryotic translation initiation factor involved in directing ribosomes to the cap structure of mRNAs. EIF4E is part of the EIF4F pre-initiation complex, which is made up of EIF4E, and EIF4G. Almost all cellular proteins require EIF4E in order to be translated into protein. EIF4E binds the first nucleotide on the 5' end of an mRNA molecule (known as the cap): a 7-Methylguanosine (m7G). It sandwiches m7G between 2 tryptophan residues, and other amino acids that are involved in the binding.

Many studies report that eIF4E is overexpressed in almost 100% of tumors within the breast, head, neck, and colon. Several retrospective studies indicate that eIF4E overexpression is correlated with poor prognosis. Reported data indicate that the inhibition of eIF4E in tumor cell lines and xenograft models impairs tumor growth and induces apoptosis; eIF4E, therefore, can be considered a valuable target for cancer therapy. Targeting the cap-binding pocket of eIF4E should represent a way to inhibit all the eIF4E cellular functions.

Human Recombinant EIF4E is expressed in E. Coli as a single, non-glycosylated polypeptide chain containing 237 amino acids, EIF4E (1-217 a.a.) with a N-terminal His-Tag. A fragment of 80 residues of EIF4G containing EIF4E binding domain is co-expressed with EIF4E. The binary complex is purified by affinity, ion exchange, and gel filtration chromatographic techniques. We also offer 4E-BP1 peptide or its complex with eIF4E for binding study.

The eIF4E proteins described above provide a method to select and develop compounds that specifically inhibit eIF4E/4G and eIF4E/4E-BP1. To learn more about Aurora Biolabs’ eIF4E products, please visit our website at https://aurorabiolabs.com/recombinant-human-eukaryotic-translation-initiation-factor-4e-eif4e-his-tag-538.html.