Recombinant Human PMM2 protein

**Background of PMM2 Recombinant Protein**

Phosphomannomutase 2 (PMM2) is a key enzyme encoded by the *PMM2* gene, which catalyzes the conversion of mannose-6-phosphate to mannose-1-phosphate—a critical step in N-glycosylation pathways. Glycosylation, the process of attaching carbohydrate chains to proteins, is essential for cellular functions such as protein folding, cell signaling, and immune response. Mutations in *PMM2* lead to PMM2 deficiency, the most common cause of congenital disorders of glycosylation (CDG), known as PMM2-CDG. This autosomal recessive condition manifests with multisystemic symptoms, including neurological deficits, developmental delays, and organ dysfunction, highlighting the enzyme's vital role in metabolic homeostasis.

Recombinant PMM2 protein is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to generate purified, functional enzyme for research and therapeutic exploration. Its production enables detailed study of PMM2’s structure, catalytic mechanisms, and interactions, aiding in understanding the molecular basis of PMM2-CDG. Additionally, recombinant PMM2 serves as a tool for screening potential therapeutics, such as pharmacological chaperones or enzyme replacement strategies, aimed at restoring enzymatic activity in affected patients.

Efforts to develop PMM2-targeted therapies are ongoing, with recombinant protein-based approaches offering promise for addressing the root cause of PMM2-CDG. Beyond therapeutics, recombinant PMM2 is utilized in diagnostic assays to assess enzyme activity in patient samples, enhancing early detection and personalized management. Overall, PMM2 recombinant protein represents a cornerstone for advancing both basic science and clinical solutions for glycosylation disorders.