Technical Articles

The time-resolved fluorescence resonance energy transfer (TR-FRET) technology combines the dual advantages of time-resolved fluorescence detection and fluorescence resonance energy transfer, providing an efficient homogeneous detection solution for the precise quantification of cyclic guanosine monophosphate (cGMP).

The histidine tag is one of the most widely used affinity tags in recombinant proteins, consisting of 6 to 10 consecutive histidine residues, typically fused to the N-terminus or C-terminus of the target protein.

IgG is the most abundant and functionally core antibody molecule in human humoral immunity, featuring a Y-shaped tetrapeptide chain glycoprotein structure composed of two heavy chains and two light chains connected by disulfide bonds, with a molecular weight of approximately 150 kDa.

In 2001, the concept of PROTAC was first proposed, which involves using bifunctional ligands to specifically bind to target proteins while recruiting E3 ligases for ubiquitination, ultimately leading to the degradation of the target proteins.

Targeted protein degradation technology has become a key research direction in the field of chemical biology. Among these, PROTAC technology achieves selective degradation of specific proteins by inducing interactions between the target protein and E3 ubiquitin ligase.

Targeted protein degradation technologies have made significant progress in the fields of chemical biology and drug discovery in recent years. Among them, PROTAC technology achieves specific ubiquitination and proteasomal degradation of target proteins by inducing proximity between the target protein and E3 ubiquitin ligase.

BCL-xL is an important anti-apoptotic protein in the BCL-2 family, overexpressed in various cancer cells, and is a well-established therapeutic target for anti-tumor effects.

Targeted protein degradation is a rapidly evolving therapeutic modality that works by harnessing intracellular degradation pathways to eliminate disease-causing proteins. The fundamental principle involves redirecting E3 ligases to ubiquitinate and degrade target proteins that would not normally be recognized or bound.

IRAK4 is a key adaptor molecule in the Toll-like receptor and IL-1 receptor signaling pathways. TLR and IL-1R share conserved TIR domains and activate similar signaling pathways.

KRAS, a core member of the small GTPase family, loses its endogenous GTP hydrolysis activity due to the G12V mutation, causing the protein to remain locked in an activated conformation and thereby driving constitutive activation of downstream signaling pathways.