These products enable clinically-significant glycan biomarker targeting for human health advancement. Glycan-based biomarkers are particularly important for disease diagnosis and treatment, yet the lack of glycan-specific reagents and tools presents a challenge. Our innovative glycoscience technologies present a solution that will advance critical research and clinical applications.
Lectenz Bio’s mission is to develop technologies that enable novel glycoscience applications, provide services that enhance glycan biomarker detection, and deliver tools that advance research and clinical applications.
The company’s core competencies in high-performance computing (HPC), digital biology, and unique wet lab expertise provide the scientific foundation for the development of the Lectenz® and GlycoSense™ technology platforms.
Advantages of Lectenz® and GlycoSense™ technologies (patents issued and pending) include:
- Each Lectenz® reagent is engineered from a carbohydrate-processing enzyme, forming a suite of novel and highly specific reagents for glycan detection and/or enrichment.
- GlycoSense TM technology measures binding between glycans and glycan-specific reagents conjugated to multiplex microspheres using flow cytometry, which is rapid, simple, and does not require highly trained personnel or specialized equipment.
- Combined Lectenz® and GlycoSenseTM products offer a robust, unique, and cost-effective solution to current bottlenecks in glycomics and glycoprofiling and are intended to greatly simplify the traditional workflow associated with glycoprofiling while delivering superior performance. Thus, these products will provide quality assurance during biomanufacturing thereby reduce the time and costs associated with meeting current FDA and EMA requirements for glycoprofile characterization of biologics and biosimilars.
APPLICATIONS FOR LECTENZ® AND GLYCOSENSETM PRODUCTS
|Infection & Inflamation|
|Congenital Disorders of Glycosylation|
|Glycoprofiling of therapeutic biopharmaceuticals|
|Process Analytical Technology|
|Potential diagnostics for altered glycosylation in disease states|