Recombinant Human PLAC1 protein

Gel4 recombinant protein is a engineered biomaterial derived from gelatin, a natural polymer obtained through partial hydrolysis of collagen. As a structural protein, collagen provides critical extracellular matrix (ECM) support in tissues, but its immunogenicity and variability in animal-derived forms limit clinical applications. Gel4 addresses these challenges through recombinant DNA technology, where specific collagen-like sequences are designed and expressed in microbial or mammalian host systems like *E. coli* or CHO cells. This process ensures precise control over molecular weight, amino acid composition, and physicochemical properties.

Unlike traditional gelatin, Gel4 lacks animal-derived contaminants and exhibits batch-to-batch consistency, making it suitable for biomedical applications. Its design often incorporates cell-binding motifs (e.g., RGD sequences) to enhance bioactivity while maintaining thermal reversibility—a key feature enabling temperature-dependent sol-gel transitions for injectable therapies. Researchers optimize its expression and purification protocols to achieve high yields of soluble, low-immunogenicity protein.

Gel4 is widely explored in tissue engineering scaffolds, drug delivery systems, and 3D bioprinting due to its tunable mechanical strength and biodegradability. It supports cell adhesion, proliferation, and differentiation, particularly in skin regeneration, cartilage repair, and neural interfaces. Recent studies also investigate its hybrid use with synthetic polymers to balance biocompatibility and structural stability. As regulatory frameworks evolve for recombinant biomaterials, Gel4 represents a promising alternative to conventional gelatin, aligning with the demand for sustainable, customizable, and ethically sourced medical materials. Ongoing research focuses on functionalizing Gel4 with growth factors or nanoparticles to expand its therapeutic potential.

PLAC1 (Placenta-Specific 1) is a cancer-testis (CT) antigen initially identified for its restricted expression in placental trophoblasts during embryonic development. Its gene, located on the X chromosome, encodes a secreted or membrane-associated protein involved in cell proliferation and differentiation. While physiologically silent in most adult tissues, PLAC1 is aberrantly reactivated in various cancers, including breast, gastric, and ovarian cancers, making it a potential biomarker and therapeutic target.

Recombinant PLAC1 protein is produced using biotechnological systems like Escherichia coli or mammalian cell cultures. Bacterial systems offer cost-effective production but may lack post-translational modifications, whereas eukaryotic systems better mimic native protein structures. This engineered protein enables functional studies to decipher PLAC1's dual role in cancer progression—acting as both an oncogenic driver through EGFR/MAPK pathway activation and a tumor suppressor via p53 regulation in certain contexts.

Research applications include:

1. Developing PLAC1-targeted antibodies for diagnostic assays

2. Investigating its immunogenicity for cancer vaccine development

3. Studying molecular interactions in tumor microenvironment modulation

4. Exploring its role in drug resistance mechanisms

Current challenges involve understanding tissue-specific expression regulation and resolving conflicting data about its pro-/anti-tumor functions. Preclinical studies using PLAC1-directed CAR-T cells and antibody-drug conjugates show promising antitumor activity, highlighting its translational potential. As a CT antigen with limited normal tissue expression, PLAC1 remains attractive for minimizing off-target effects in cancer immunotherapy strategies.