Product Launch | LMNG–The new generation of high-stability detergent specifically designed for membrane proteins, addressing key challenges in GPCR and ion channel research

Membrane proteins represent core targets in drug discovery; however, their strong hydrophobicity often leads to denaturation and aggregation upon separation from the cell membrane. Techniques such as cryo-electron microscopy, protein crystallization, and target interaction assays frequently encounter obstacles due to protein inactivation or background interference. Today, we are officially launching Lauryl Maltose Neopentyl Glycol (LMNG/MNG-3), a high-performance nonionic detergent. Leveraging its unique dual-head, dual-tail neopentyl glycol backbone structure, this compound effectively combines high solubilization capacity with conformational stabilization, offering comprehensive compatibility with cutting-edge structural biology and high-throughput drug screening workflows, thereby providing a stable and reliable solution for the study of complex membrane proteins.

I. Core Product Structure: Specifically designed for unstable membrane proteins

LMNG belongs to the MNG class of novel nonionic surfactants; distinct from traditional mono-sugar-based surfactants, it employs a symmetrical dual-head, dual-tail n-pentylene glycol molecular backbone—where a double maltose hydrophilic head is paired with a double lauryl hydrophobic tail—to form a dense, flexible, and controllable micelle shell.

This approach not only enables efficient isolation of poorly soluble membrane proteins—such as GPCRs, ion channels, and SLC transporters—from cell membranes, but also mimics the native lipid microenvironment, thereby preserving the protein's native spatial conformation and ligand-binding activity to the greatest extent possible, while significantly reducing the probability of in vitro degradation and aggregation.

Basic Molecular Information

• CAS Number: 1257852-96-2

• Molecular formula: C₄₇H₈₈O₂₂

• Molecular weight: 1005.19

II. Three core advantages that outperform traditional detergents by a wide margin

1. ≥99% ultra-high purity, suitable for ultra-high-resolution structural determination

Utilizing a rigorous HPLC purification process, the product achieves stable purity of ≥99% with extremely low levels of nucleic acids, proteins, and small-molecule impurities; the UV absorbance at 260/280/340 nm is strictly controlled, eliminating any background interference from impurity signals—thereby providing optimal support for cryo-electron microscopy (Cryo-EM) and high-resolution X-ray crystallography, ensuring uniform particle imaging and exceptionally low noise levels, which facilitates the acquisition of atomic-scale fine structural details.

2. Ultra-low CMC (~0.01 mM), enabling long-term stability of micelles

The critical micelle concentration is only 0.01 mM (0.001% w/v aqueous solution), which is significantly lower than that of conventional detergents such as DDM and OG; the dense micelle structure resists dissociation, markedly prolongs the in vitro half-life of membrane proteins, reduces protein inactivation losses during purification, incubation, and crystallization processes, and substantially improves the success rate of experiments.

3. Gentle conformational protection covering all high-difficulty targets

The unique double-branched symmetric architecture exerts mild force without disrupting the flexible structure of the transmembrane region, ensuring optimal compatibility with highly unstable membrane proteins such as G protein-coupled receptors, voltage-gated ion channels, and transporters; it fully preserves the ligand-binding function throughout the process, making it ideal for molecular interaction studies and drug screening experiments.

III. Strict quality control standards ensure that the performance of each batch remains stable and controllable.

LMNG undergoes comprehensive factory-level performance testing with standardized physicochemical parameters, showing no significant batch-to-batch variation:

Storage and Transportation Requirements

• Storage: Store at-20°C, protected from light, in a sealed container and under dry conditions.

• Transportation: Blue Ice Transport

IV. All-scenario applications covering the entire value chain of membrane protein research

1. Single-particle structure determination by cryo-electron microscopy (Cryo-EM)

Membrane protein–ligand complex samples: the preferred choice for sample preparation; features uniform micelle size, a clean electron microscopy background, reduced particle overlap and aggregation, and significantly enhanced three-dimensional reconstruction resolution.

2. Extraction and purification of unstable membrane proteins

Mild solubilization of GPCRs, ion channels, and transporters; affinity chromatography; and gel filtration purification—all of which enhance the recovery yield and activity retention of target proteins.

3. Protein crystallization & X-ray diffraction

Stabilizes protein flexible regions, reduces conformational heterogeneity, promotes the growth of high-quality three-dimensional protein crystals, and optimizes the quality of diffraction data.

4. Drug target screening and molecular interaction analysis

Compatible with SPR, BLI surface plasmon resonance, and DSF thermal shift assays; stabilizes the active site of target proteins, effectively restores the binding affinity between drug molecules and membrane proteins, and facilitates lead compound screening.

V. Spot Specifications and Procurement Information

Standard Spot SKU

If you require custom kilogram-grade industrial or platform bulk packaging solutions, please visit the "Contact Us" page on our official website to submit your request; we support customized batch supply and dedicated technical support services.