SERPINE1 Antibodies

Structure of SERPINE1

SERPINE1 is a glycoprotein with a molecular weight of approximately 45 kDa. The actual measured value often fluctuates within the range of 42 to 55 kDa due to differences in glycosylation.

This protein is composed of 379 amino acids, and its three-dimensional structure is characterized by a central β -barrel-shaped fold. The active center contains a unique flexible hinge region that can trap the target protease. The key functional sites are composed of arginine-346 and histidine-343 on the reaction center ring. These two residues achieve specific and irreversible inhibition of plasminogen activators through steric hindrance effects.

Fig. 1 SERPINE1 in Gastric Cancer Exosomes Drives Macrophage M2 Polarization.¹

Key structural properties of SERPINE1:

• Central β -barrel-shaped folded core structure
• Highly flexible active center ring (reaction center ring)
• "Entrapment" mechanism of protease binding sites
• Key arginine - 346 residues mediated irreversible inhibition

Functions of SERPINE1

The main function of SERPINE1 (plasminogen activator inhibitor-1) is to maintain vascular homeostasis by inhibiting the fibrinolytic system. However, it is also widely involved in a variety of pathophysiological processes, including tissue remodeling, inflammatory responses and tumor progression.

The inhibitory kinetics of SERPINE1 exhibits a unique "trapping" mechanism. Its interaction with the target protease shows a slow binding but irreversible characteristic, which contrasts sharply with the rapid reversible equilibrium of typical serine protease inhibitors, establishing its core position in thrombotic and fibrotic diseases.

Applications of SERPINE1 and SERPINE1 Antibody in Literature

1. Zhang, Dan, et al. "Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation." Molecular Cancer 23.1 (2024): 70. https://doi.org/10.1186/s12943-024-01985-1

Studies have shown that senescent tumor cells induced by anti-cancer treatment release extracellular vesicles rich in SERPINE1. SERPINE1 in these vesicles can bind to p65, activating the NF-κB signaling pathway and thereby promoting the progression of colorectal cancer. Inhibiting SERPINE1 can block this effect.

2. Ye, Zhenzhen, et al. "Gastric cancer-derived exosomal let-7 g-5p mediated by SERPINE1 promotes macrophage M2 polarization and gastric cancer progression." Journal of Experimental & Clinical Cancer Research 44.1 (2025): 2. https://doi.org/10.1186/s13046-024-03269-4

Studies have found that gastric cancer cells activate the JAK2/STAT3 pathway by highly expressing SERPINE1, promoting the packaging of let-7g-5p into exosomes. After the exosome is taken up by macrophages, let-7g-5p enhances STAT3 phosphorylation by inhibiting SOCS7, thereby driving macrophages to polarize to the M2 type and promoting tumor progression.

3. Wang, Luning, et al. "RBM4 regulates cellular senescence via miR1244/SERPINE1 axis." Cell death & disease 14.1 (2023): 27. https://doi.org/10.1038/s41419-023-05563-z

Studies have shown that the deletion of RNA-binding protein RBM4 promotes the degradation of primary miR-1244, resulting in a reduction of its mature bodies. This weakens the inhibitory effect of miR-1244 on the key aging factor SERPINE1, upregulates the expression of SERPINE1, and ultimately induces the senescence of lung cancer cells and inhibits tumor progression.

4. Pavón, Miguel Angel, et al. "uPA/uPAR and SERPINE1 in head and neck cancer: role in tumor resistance, metastasis, prognosis and therapy." Oncotarget 7.35 (2016): 57351. https://doi.org/10.18632/oncotarget.10344

Studies have shown that in head and neck squamous cell carcinoma, uPA/uPAR and its inhibitor SERPINE1, although functionally contradictory, are both highly expressed and can promote tumor metastasis and lead to a poor prognosis. The mechanism lies in the fact that SERPINE1 can activate pro-cancer signals independently of the uPA inhibitory function. Both can serve as prognostic biomarkers and potential therapeutic targets.

5. Li, Lingqin, et al. "Identification and validation of SERPINE1 as a prognostic and immunological biomarker in pan-cancer and in ccRCC." Frontiers in pharmacology 14 (2023): 1213891. https://doi.org/10.3389/fphar.2023.1213891

Studies have shown that SERPINE1 is abnormally highly expressed in various cancers and is associated with a poor prognosis. Its expression is regulated by gene copy number amplification and DNA hypomethylation. Studies have confirmed that SERPINE1 plays a key role in the malignant progression of tumors and immunosuppression by influencing immune regulation, immune cell infiltration and tumor mutational burden.

Creative Biolabs: SERPINE1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SERPINE1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SERPINE1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our SERPINE1 antibodies, custom preparations, or technical support, contact us at email.