Recombinant Human Beta-amyloid 38 protein

VSIG2 (V-set and immunoglobulin domain-containing protein 2) is a transmembrane protein belonging to the immunoglobulin (Ig) superfamily, characterized by its extracellular V-set and Ig-like domains. Initially identified as a complement receptor-related protein, VSIG2 has garnered attention for its potential role in immune regulation and cancer biology. It is expressed in various tissues, including the placenta, gastrointestinal tract, and immune cells, and is implicated in cell-cell adhesion, signaling, and modulation of immune responses. Recent studies highlight its involvement in the tumor microenvironment, where it may act as a co-inhibitory molecule to suppress T-cell activity, akin to established immune checkpoints like PD-1/PD-L1.

Recombinant VSIG2 protein is engineered using expression systems (e.g., mammalian cells, HEK293) to produce soluble, high-purity forms of the extracellular domain. This enables functional studies to dissect its interactions with ligands, receptors, or antibodies. Researchers utilize recombinant VSIG2 to explore its immunosuppressive mechanisms, particularly its ability to bind putative receptors on immune cells and inhibit effector functions, which may contribute to tumor immune evasion. Its overexpression in certain cancers (e.g., ovarian, colorectal) correlates with poor prognosis, reinforcing its therapeutic relevance.

In drug development, recombinant VSIG2 serves as a critical tool for screening monoclonal antibodies or small molecules aimed at blocking its immunosuppressive activity. Preclinical models demonstrate that targeting VSIG2 enhances anti-tumor immunity, suggesting its potential as a novel checkpoint inhibitor. Additionally, recombinant VSIG2 aids in biomarker discovery and structural studies to map functional epitopes. While most research remains in early stages, VSIG2’s unique positioning within immune regulatory networks underscores its promise for advancing cancer immunotherapy and understanding immune tolerance pathways.

Beta-amyloid 38 (Aβ38), a 38-amino acid isoform of the amyloid-β peptide, is a less-studied variant compared to the more commonly referenced Aβ40 and Aβ42 in Alzheimer’s disease (AD) research. Derived from the sequential proteolytic cleavage of amyloid precursor protein (APP) by β- and γ-secretases, Aβ38 represents a shorter C-terminal truncation of the Aβ peptide family. Its production is linked to alternative γ-secretase activity, particularly associated with the “α-like” cleavage pathway, which may compete with the generation of longer, more aggregation-prone species like Aβ42.

While Aβ42 is a major component of amyloid plaques in AD brains, Aβ38 exhibits distinct biophysical properties. Studies suggest it is more soluble and less prone to aggregation, potentially acting as a “protective” fragment by modulating the toxicity or aggregation kinetics of longer Aβ species. However, its precise physiological or pathological role remains debated. Elevated Aβ38 levels have been observed in certain genetic mutations (e.g., presenilin-1 variants) and experimental models, hinting at its relevance in amyloidogenic processing.

Recombinant Aβ38 is synthesized in vitro using bacterial or mammalian expression systems, enabling standardized studies of its structure, interactome, and biological effects. Researchers employ it to investigate γ-secretase modulation, evaluate therapeutic strategies aiming to shift Aβ production toward shorter isoforms, or explore its potential as a biomarker. Despite its lower prominence in AD pathology, Aβ38 serves as a critical tool for understanding the complexity of APP processing and the balance between neurotoxic and neuroprotective Aβ species. Ongoing research aims to clarify its role in disease mechanisms and therapeutic development.