Recombinant Human MHCG protein

**Background of PLA2G3 Recombinant Protein**

Phospholipase A2 Group III (PLA2G3), a member of the secreted phospholipase A2 (sPLA2) family, is an enzyme that hydrolyzes phospholipids at the *sn-2* position to release free fatty acids (e.g., arachidonic acid) and lysophospholipids. These products serve as precursors for bioactive lipid mediators, such as prostaglandins and leukotrienes, which play critical roles in inflammation, immune responses, and cellular signaling. PLA2G3. also termed sPLA2-III, is distinct in its structural features, including a long N-terminal domain and a central sPLA2 catalytic domain, enabling unique substrate interactions and regulatory functions.

Biologically, PLA2G3 is implicated in lipid metabolism, membrane remodeling, and pathological conditions like allergic inflammation, cancer, and metabolic disorders. Studies suggest it influences epidermal hyperplasia and skin barrier function, with knockout models revealing its role in mitigating hyperimmunoglobulin E syndrome-like symptoms. Additionally, PLA2G3 may regulate extracellular vesicle release and intercellular communication.

Recombinant PLA2G3 protein is produced via heterologous expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications and enzymatic activity. This engineered protein is pivotal in functional studies, inhibitor screening, and elucidating mechanisms of lipid-mediated signaling. Its availability accelerates research into sPLA2-driven diseases and supports therapeutic development targeting lipid pathways.

Overall, PLA2G3 recombinant protein serves as a vital tool for dissecting the enzyme’s biological roles and exploring its therapeutic potential in inflammation-related and metabolic diseases.

**Background of MHCG Recombinant Protein**

MHCG (Major Histocompatibility Complex Class G) recombinant protein is a genetically engineered molecule derived from the human MHC class Ib gene, *HLA-G*, which plays a critical role in immune modulation and tolerance. Unlike classical MHC class I molecules, HLA-G exhibits limited polymorphism and is predominantly expressed in immune-privileged sites, such as the placenta during pregnancy, where it suppresses maternal immune responses to fetal tissues. This unique function has made HLA-G a key focus in reproductive immunology and transplantation research.

Recombinant MHCG proteins are typically produced using expression systems like *E. coli*, yeast, or mammalian cells, enabling large-scale production of soluble HLA-G isoforms (e.g., HLA-G1. HLA-G5). These proteins retain the functional α-chain structure, often complexed with β2-microglobulin and peptide antigens, mimicking natural HLA-G interactions with immune receptors such as inhibitory receptors LILRB1 and LILRB2 on NK cells, T cells, and antigen-presenting cells.

Research highlights MHCG’s role in promoting immune tolerance by dampening cytotoxic activity, inhibiting inflammatory cytokine release, and inducing regulatory T cells. These properties have spurred interest in therapeutic applications, including preventing organ transplant rejection, managing autoimmune diseases, and improving outcomes in pregnancy-related complications like recurrent miscarriage. Additionally, tumor cells often exploit HLA-G expression to evade immune surveillance, making recombinant MHCG a tool for studying cancer immunotherapies.

Despite its potential, challenges remain in standardizing isoform-specific functions and optimizing delivery mechanisms. Ongoing studies aim to clarify HLA-G’s dual roles in tolerance and pathology, driving innovations in biotherapeutic design. MHCG recombinant protein thus represents a bridge between fundamental immunology and clinical translation, offering avenues for targeted immune intervention.