Recombinant Human 3 protein

INPP4A (inositol polyphosphate-4-phosphatase type I) is a phosphatase enzyme encoded by the *INPP4A* gene, primarily involved in regulating phosphoinositide signaling pathways. It catalyzes the hydrolysis of the 4-phosphate group from phosphatidylinositol 3.4-bisphosphate [PI(3.4)P2] and phosphatidylinositol 4.5-bisphosphate [PI(4.5)P2], key lipid secondary messengers that modulate cellular processes such as proliferation, survival, and apoptosis. Structurally, INPP4A contains a conserved phosphatase domain and a C-terminal catalytic domain, enabling its substrate specificity and enzymatic activity.

Recombinant INPP4A protein is engineered in vitro using expression systems like mammalian, insect, or bacterial cells to produce a purified, functional form of the enzyme for research applications. Its production often involves tagging (e.g., His-tag) to facilitate purification and detection. Studies highlight INPP4A's dual roles in disease: as a tumor suppressor in cancers (e.g., breast, prostate) by antagonizing PI3K/AKT/mTOR signaling, and paradoxically, as a promoter of metastasis in certain contexts. It also links to neurodegenerative disorders (e.g., Alzheimer’s disease) through interactions with amyloid-beta and tau proteins, and metabolic syndromes via insulin signaling regulation.

Researchers utilize recombinant INPP4A to dissect its enzymatic mechanisms, substrate interactions, and structural features. It serves as a tool for drug screening, pathway analysis, and functional studies in cellular models. However, challenges remain in understanding its tissue-specific roles and post-translational modifications. Overall, recombinant INPP4A provides a critical resource for advancing insights into phosphoinositide metabolism and therapeutic targeting in diverse diseases.

Recombinant proteins, engineered through genetic modification techniques, represent a cornerstone of modern biotechnology. The concept emerged in the 1970s with the development of recombinant DNA technology, enabling scientists to transfer genes encoding specific proteins into host organisms. This breakthrough addressed critical limitations in obtaining therapeutic proteins from natural sources, which were often scarce, expensive, or contaminated with pathogens.

The production process involves isolating a target gene, inserting it into expression vectors (typically plasmids), and introducing these into host cells like bacteria (E. coli), yeast (Pichia pastoris), or mammalian cells (CHO cells). These modified organisms then synthesize the desired protein through their cellular machinery. Insulin became the first commercially available recombinant protein in 1982. revolutionizing diabetes treatment by replacing animal-derived insulin.

Advancements in expression systems, purification technologies (e.g., affinity chromatography), and protein engineering (including fusion tags and glycoengineering) have dramatically expanded applications. Today, recombinant proteins are vital in therapeutics (monoclonal antibodies like adalimumab, vaccines like HPV vaccine), research tools (enzymes for PCR), industrial processes (detergent proteases), and diagnostics (COVID-19 antigen tests).

Current research focuses on improving production yields, enhancing protein stability, and developing novel expression platforms including plant systems and cell-free synthesis. Challenges remain in producing complex proteins requiring post-translational modifications, driving the adoption of CRISPR-edited cell lines and AI-assisted protein design. The global recombinant protein market continues to grow, fueled by increasing demand for biologics and personalized medicine approaches.