protein tagging

Targeted Protein Degradation (TPD) is a novel and promising approach to drug development. It shows great potential for targeting proteins traditionally considered "undruggable" due to the lack of enzymatic function and absence of binding sites by tagging them for degradation or recruiting natural degradation mechanisms.

Molecular glues are a type of small-molecule degraders that primarily induce novel interactions between E3 ubiquitin ligases and target proteins, forming ternary complexes that lead to protein ubiquitination and subsequent proteasomal degradation. Compared with PROTACs, molecular glues generally have lower molecular weights, higher cell permeability, and better drug-like properties. Additionally, the design of molecular glues is relatively simple, without the requirements for complex linkers and ligand optimization. As a result, molecular glues have gradually emerged as a promising therapeutic approach for various diseases.

Multiple types of molecular glues have been reported previously. Analysis of co-crystal complex structures reveals that CRBN-related molecular glues are more versatile. Therefore, MCE researchers select active molecules related to these targets as probes for artificial intelligence (AI) screening.Subsequently, molecular docking technology was used to verify whether the screened molecules retained the key pharmacophore features. Ultimately, we obtained 317 molecular glue analogs, and these compounds serve as powerful tools for the research of molecular glues.

The discovery of hit molecule is a cornerstone of drug development. Among the diverse tools available, DNA-encoded libraries have emerged a revolutionary platform for high-throughput screening. Compared with traditional HTS, DEL features shorter screening processes, lower costs, simpler assays, and larger library capacities.

DEL Construction utilizes split-and-pool synthesis, a combinatorial chemistry approach that involves iterative splitting, reaction, and pooling. This strategy enables rapid, exponential assembly of fragments in minimal steps without the need for individual compound synthesis andassoicicated isolation or purification steps, thus greatly reducing overall costs. The technology enables simultaneous affinity screeningof massive compound collections to target proteins in a single step. By coupling chemical structures with unique DNA barcodes, each compound is tagged with a distinct DNA sequence for convenient tracking and decoding.DELs readily enable the construction and efficient screening of libraries containing millions to billions of compounds. As a result, DEL screening combines the dual advantages of high efficiency and low cost, making DEL a transformative technology in modern drug discovery.

The DEL kit consists of 50 independent libraries with a total scale of 100 billion compounds. It is constructed through stepwise combinatorial chemistry strategies involving 2-, 3-, and 4-round synthesis. By employing diverse scaffolds and flexible linking strategies, it encompasses various ring systems, linear frameworks, and heterocyclic structures. Screening can be achieved solely through affinity, independent of target-specific activity detection methods. This library is suitable for DEL screening against a wide range of targets.

MCE Ni-NTA His-Tag Purification Agarose, a 6% highly cross-linked agarose reagent, enables high-yield, high-purity purification of his-tagged proteins.

MCE Ni-IDA Agarose can be used for the detection and purification of His-tag proteins.

MCE Anti-Flag Magnetic Beads are used for immunoprecipitation (IP) of specific Flag-tagged (DYKDDDDK) proteins expressed in bacterial and mammalian cells and in vitro expression systems, and also suitable for Co-immunoprecipitation and purification of Flag-tagged protein. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Anti-YFP Affinity Gel can be used for the detection and purification of proteins tagged with GFP and EGFP and IP assays.

MCE Anti-Flag Affinity Gel is used for immunoprecipitation (IP) or protein purification of specific Flag-tagged (DYKDDDDK) proteins expressed in bacterial and mammalian cells and in vitro expression systems.

MCE Affinity Chromatography (AC) Columns are designed for purification of recombinant proteins with different tags, enzymes, antibodies, antigens and nucleic acids.

MCE Ni-NTA Magnetic Agarose Beads can be used for the detection and purification of His-tag proteins from various expression sources.

MCE Ni-IDA Magnetic Agarose Beads can be used for the detection and purification of His-tag proteins from various expression sources.

MCE Anti-V5 Magnetic Beads are well suited for the detection and purification of V5-tagged fusion proteins, as well as for applications such as immunoprecipitation (IP) and co-immunoprecipitation (Co-IP). The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Glutathione Agarose, a 4% highly cross-linked agarose reagent, enables high-yield, high-purity purification of GST-tagged proteins.

MCE Glutathione Magnetic Agarose Beads have high protein-binding capacity and stability, making it ideal for high performance purification of GST-tagged fusion proteins expressed in E. coli, yeast, insect and mammalian expression systems.

MCE Ni-NTA 6FF Prepacked Column is ideal for high performance purification of polyhistidine-tagged proteins expressed in E.coli, yeast, insect and mammalian expression systems.

MCE Chelating Agarose (IDA) 6FF allows flexible chelation with metal ions such as Zn²⁺, Ni²⁺, or Cu²⁺, and is suitable for the purification of His-tagged recombinant proteins expressed in bacterial, mammalian, insect, and baculovirus systems.

MCE Anti-GST Magnetic Beads are used for immunoprecipitation (IP) of specific GST-tagged proteins expressed in bacterial and mammalian cells and in vitro expression systems. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Anti-His Magnetic Beads are used for immunoprecipitation (IP) of specific His-tagged proteins expressed in bacterial and mammalian cells and in vitro expression systems. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

Anti-MBP Magnetic Beads are suitable for the detection and purification of MBP-tagged fusion proteins, as well as for immunoprecipitation (IP) and co-immunoprecipitation (Co-IP) applications. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Anti-HA Magnetic Beads are used for immunoprecipitation (IP) of specific HA-tagged proteins expressed in bacterial and mammalian cells and in vitro expression systems.The 1 mL volume is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Anti-c-Myc Magnetic Beads are used for immunoprecipitation (IP) of specific c-Myc-tagged proteins expressed in bacterial and mammalian cells and in vitro expression systems. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE Anti-HA Magnetic Beads (1 μm) are used for immunoprecipitation (IP) of specific HA-tagged proteins expressed in bacterial and mammalian cells andin vitro expression systems. The 1 mL is defined as the base specification. All larger sizes correspond to incremental volumes of this base.

MCE IMAC Agarose (NTA) 6FF is prepared by covalently coupling tetradentate nitrilotriacetic acid (NTA) to an agarose matrix. It features high binding capacity, excellent specificity, and superior ligand stability. The resin allows flexible chelation with metal ions such as Zn²⁺, Ni²⁺, or Cu²⁺, and is suitable for the purification of His-tagged recombinant proteins expressed in bacterial, mammalian, insect, and baculovirus systems.