Explore our applications

Group of Students Working at the Laboratory

Industry-Trusted Biotechnology Company and CRO

Advance your biomedical research industry with help from CASSIA LLC. Founded in 2004, we are a privately held biotechnology company and clinical research organization (CRO) specializing in green chemo-enzymatic synthesis solutions for preparing stable isotope-labeled (D, C-13, N-15, O-17/18) metabolites, proteins, nucleic acids, and their analogs.

Leveraging our unique core technology platforms and expertise, we bring responsible, cost-effective, and creative solutions to a variety of basic, translational, and biomedical research applications, such as:

MS
NMR
Assay Development
Metabolic Research

Interior of Clean Modern White Medical or Chemical Laboratory Background

Our Facility

CASSIA LLC laboratories are located in an eight-building, 150,700 sq. ft. research and development (R&D) business park in the Mira Mesa region of San Diego, CA. We occupy 1580 sq. ft. and are capable of carrying out both basic and applied research in:

Molecular Biology
Biocatalysis
Organic Synthesis
Protein and Nucleic Acid Production

Contact us today to learn more about our biotechnology company and the products and services we provide.

Explore our Latest Application Using Stable Isotope Labeled Nucleotide-Sugars

Pre-B Cell Receptor Acts as a Selectivity Switch for Galectin-1 at the Pre-B Cell Surface

Summary – Galectins are glycan-binding proteins translating the sugar-encoded information of cellular glycoconjugates into physiological activities, including immunity, cell migration, and signaling. Galectins also interact with non-glycosylated partners in the extracellular milieu, among which the pre-B cell receptor (pre-BCR) during B cell development. Here, we perform NMR experiments on native membranes to monitor Gal-1 binding to physiological cell surface ligands. We show that pre-BCR interaction changes Gal-1 binding to glycosylated pre-B cell surface receptors. At the molecular and cellular levels, we identify α-2,3-sialylated motifs as key targeted epitopes. This targeting occurs through a selectivity switch increasing Gal-1 contacts with α-2,3-sialylated poly-N-acetyllactosamine upon pre-BCR interaction. Importantly, we observe that this switch is involved in the regulation of pre-BCR activation. Altogether, this study demonstrates that interactions to non-glycosylated proteins regulate the glycan-decoding functions of galectins at the cell surface. [Cell Reports 2024, 48(8), 114541.]