Peptide Preparation Methods TRIZ Cases

A nucleic acid conjugate combines ligand coding sequences with sortase recognition tags to enable single-step protein purification and site-specific ligation.

Sequential acid and base treatments recover phosphorus and proteins from manure, reducing environmental pollution.

Laureth-9 replaces Triton X-100 to achieve viral clearance while maintaining environmental compatibility.

A tandem purification system combines affinity and ion exchange resins in series to process proteins continuously.

Enzymatic hydrolysis breaks down viscous mucilage to enable ultrafiltration, producing a phytoestrogen-free protein powder with 21-32% content.

A thermal shift assay detects ligand binding by separating soluble from insoluble proteins after heat treatment.

A biomolecular labeling reagent uses a rigid aromatic backbone to constrain fluorophore orientation and minimize inter-label interactions.

Optimized elution pH separates ISVD monomers from aggregates during Protein A chromatography, reducing aggregate content below 5%.

A soybean variety uses genetic transformation to introduce specific traits.

Inverted transmembrane enzymes localize active sites to the cytoplasm, resolving contradictions between high production capacity and disulfide bond formation.

Controlled oxidation in urea buffers resolves folding contradictions, yielding high-purity three-finger neurotoxins.

Engineered VHH ligands resolve Protein A elution bottlenecks for bispecific antibodies and ADCs.

Addressable antibody arrays detect intracellular truncated receptor activation states in circulating tumor cells.