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Protein-RNA interaction-Pull‑down

Protein-RNA interactions are central mechanisms of gene expression regulation, governing RNA processing, transport, translation, and degradation.

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Protein-DNA interaction-Pull-down

A biotin‑labeled DNA probe is designed to target a specific genomic or regulatory region of interest.

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Protein-DNA interaction-ChIP (Chromatin Immunoprecipitation)

Chromatin Immunoprecipitation (ChIP) is a classical epigenetic technique for studying in vivo protein‑DNA interactions, serving as a core tool for deciphering gene expression regulatory mechanisms, transcription factor binding sites, and epigenetic modification landscapes.

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FRET (Fluorescence Resonance Energy Transfer)

Fluorescence Resonance Energy Transfer (FRET) is a physical process based on non-radiative dipole-dipole coupling between a donor fluorophore and an acceptor fluorophore.

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Protein-protein interaction-BiFC (Bimolecular fluorescence complementation)

Bimolecular Fluorescence Complementation (BiFC) is an imaging technique for visualizing protein-protein interactions in living cells.

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Protein‑protein interaction-LCA (Luciferase Complementation Assay)

Luciferase Complementation Assay (LCA) is a highly sensitive, high-throughput protein-protein interaction detection technology based on the principle of protein fragment complementation.

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Protein‑protein interaction-Y2H (Yeast two-hybrid)

Yeast Two-Hybrid (Y2H) is an in vivo protein-protein interaction screening technology based on the modular structure of transcription factors.

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Protein‑protein interaction-Co-IP (Co-Immunoprecipitation)

Co-IP is a classical in vivo protein-protein interaction technology developed based on the principle of Immunoprecipitation (IP).

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Protein‑protein interaction-Pull‑down

The pull-down assay is an effective in vitro technique for validating protein-protein interactions, commonly used to confirm interacting proteins identified by yeast two-hybrid systems or other screening methods.

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