Recombinant Human PTGDS protein

Prostaglandin D2 synthase (PTGDS), also known as lipocalin-type prostaglandin D synthase (L-PGDS), is a dual-function protein that plays critical roles in inflammation regulation, nervous system function, and cellular homeostasis. This 26-28 kDa enzyme catalyzes the isomerization of prostaglandin H2 (PGH2) to prostaglandin D2 (PGD2), a lipid mediator involved in sleep induction, allergic responses, and smooth muscle contraction. Beyond its enzymatic activity, PTGDS acts as a lipid transporter, binding small hydrophobic molecules like retinoids and bile pigments through its characteristic lipocalin protein structure.

The recombinant PTGDS protein has become an essential tool for biomedical research due to challenges in isolating the native protein from biological sources. Produced through heterologous expression systems (typically E. coli or mammalian cells), recombinant PTGDS maintains proper folding and enzymatic activity while ensuring batch-to-batch consistency. This engineered protein enables detailed studies of PGD2 signaling pathways and their implications in neuroprotection, circadian rhythm regulation, and pathological conditions including neurodegenerative diseases (e.g., Alzheimer's), atherosclerosis, and tumor progression.

Current research leverages recombinant PTGDS to investigate its paradoxical roles – while PGD2 exhibits pro-inflammatory effects in allergies, its dehydration product 15d-PGJ2 shows anti-inflammatory properties through PPARγ activation. The protein's structural features, including conserved cysteine residues critical for catalytic activity and substrate-binding pocket architecture, remain key focuses for drug discovery. Recombinant PTGDS also serves as a biomarker validation tool, particularly in cerebrospinal fluid analysis for neurological disorders. Ongoing studies aim to unravel its non-enzymatic functions in cellular differentiation and oxidative stress responses, highlighting its therapeutic potential across multiple disease domains.