Nuclear Hormone Receptors (NHRs) are intracellular proteins that sense steroid hormones, thyroid hormones, and other signaling molecules. By regulating gene expression and maintaining physiological homeostasis, NHRs have become important drug discovery targets for cancer, metabolic disorders, and endocrine diseases.
ICE Bioscience provides integrated biochemical and cell-based NHR assays, supporting ligand-binding characterization, coactivator recruitment, reporter-gene analysis, and emerging induced-proximity programs involving receptors such as AR and ER.
Androgen and estrogen receptors, including AR and ER, regulate hormone-responsive gene expression and are central to oncology and endocrine research.
NHR signaling contributes to metabolic homeostasis and provides opportunities for developing therapies for metabolic and endocrine disorders.
Ligand-dependent recruitment of transcriptional cofactors connects receptor binding with downstream gene-expression changes.
Fluormone-tracer competitive binding assays measure displacement of a fluorescent ligand from the receptor and support characterization of small-molecule binding affinity.
HTRF-based coactivator recruitment assays monitor receptor–coactivator interactions and provide a proximity-based readout of transcriptional activation mechanisms.
Reporter systems incorporating ligand-binding domains, DNA-binding domains, HREs, or UAS-GAL4 response elements evaluate NHR activation and inhibition in living cells.
AR and ER are increasingly explored as recruitment handles in induced-proximity and RIPTAC programs. Their ligand-binding domains provide a framework for studying bifunctional molecules that engage a nuclear hormone receptor and recruit a second target or effector protein.
Fluorescence-polarization and related binding formats can assess whether an AR- or ER-directed ligand retains receptor engagement after bifunctional design and linker incorporation.
Ternary-complex assays can distinguish independent binary binding from induced proximity between AR or ER and a recruited partner.
Reporter assays, cofactor-recruitment assays, and target-proximal biochemical readouts can be combined to evaluate the functional consequences of AR- or ER-centered induced proximity.
We value your inquiries and are here to provide you with tailored solutions for your drug discovery and development needs. Whether you have questions, require more information, or are interested in discussing potential collaborations, our team of experts is just a message away.
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Address: Bldg 16, Yd 18, Kechuang 13th St, Etown, Tongzhou Dist, Beijing, 100176, China
Email: marketing@ice-biosci.com
Tel：+86-10-67809840
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