Recombinant Mouse Thrombospondin-1 (TSP-1) (ALRP51)

Thrombospondin-1 (TSP-1, encoded by the THBS1 gene) is a 150–180 kDa calcium-sensitive, matricellular glycoprotein that is secreted into the extracellular matrix (ECM) as a complex disulfide-linked homotrimer (totaling ~450 kDa). Native TSP-1 is widely produced by platelets, endothelial cells, fibroblasts, and immune cells. It features a highly modular structure, including an N-terminal domain, a von Willebrand factor type C domain, multiple TSP type 1, 2, and 3 repeats, and a C-terminal lectin domain. Because of this multimodular architecture, TSP-1 acts as a dynamic biological modulator, regulating cellular behavior by interacting with a wide array of cell-surface receptors (e.g., CD36, CD47, integrins), growth factors, and other ECM components.

Biological Functions and Signaling Pathways TSP-1 is a highly pleiotropic protein with a well-established role as a potent endogenous inhibitor of angiogenesis. By binding to the CD36 receptor on vascular endothelial cells, TSP-1 neutralizes VEGF signaling, inhibits endothelial cell proliferation and migration, and induces cell apoptosis.

Beyond its anti-angiogenic properties, TSP-1 is a primary physiological activator of latent Transforming Growth Factor-beta (TGF-β), binding to the latency-associated peptide (LAP) to release active TGF-β, thereby driving tissue repair, remodeling, and localized fibrotic responses. Furthermore, TSP-1 binds to CD47 to dampen adaptive immune responses by inhibiting T-cell receptor (TCR) signaling and promoting regulatory T cell differentiation. It also plays vital roles in platelet aggregation, wound healing, and macrophage-mediated clearance of apoptotic cells.

The HEK293 Expression Advantage Leinco’s Recombinant Mouse TSP-1 is produced in a mammalian human embryonic kidney (HEK293) expression system. Because mature TSP-1 is a large, heavily glycosylated, and complex homotrimeric protein, the choice of expression system is critical for downstream performance.

Superior to Bacterial Systems: Bacterial expression systems (such as E. coli) cannot perform glycosylation or assemble complex multimeric structures, limiting them to producing truncated, non-glycosylated protein fragments (e.g., amino acids 19–350).

A Premier Mammalian Alternative: While some competitive full-length proteins are produced in murine myeloma (NS0) cells, HEK293 cells are globally recognized for highly efficient, stable production of complex proteins without the risk of adding immunogenic non-human glycans (such as α-Gal) that NS0 cells sometimes attach. Expression in HEK293 cells ensures the incorporation of native-like post-translational modifications, proper disulfide-linked trimerization, and accurate protein folding. This results in a functionally active, full-length protein that closely mimics natural murine TSP-1, making it the ideal choice for sensitive in vitro cell adhesion assays, receptor-binding studies, and signaling pathway research.

Q3TR40

Lyophilized

Reconstitute at 0.1-1 mg/ml using filtered deionized water. Gently mix by vortexing and/or inversion until fully dissolved. Centrifuge if necessary.

This lyophilized protein is stable for twelve months when stored at -20°C to -70°C. After aseptic reconstitution, this protein may be stored for one month at 2°C to 8°C or for three months at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles.

Ambient