Our active recombinant human plasminogen protein (PLG) is produced by expressing the gene fragment that encodes the 98-356aa region of the human PLG in E.coli. Its specific activity is 5.5x105 IU/mg, determined by an assay on anti-proliferation and anti-migration using endothelial cells in vitro and anti-angiogenesis in vivo. Its endotoxin level is below 1.0 EU/μg as determined by the LAL method. It achieves over 90% purity, as measured by SDS-PAGE.
Human PLG is a crucial protein in the fibrinolytic system, primarily responsible for the conversion of fibrin into soluble fibrin degradation products, thereby facilitating the dissolution of blood clots. It is synthesized in the liver and circulates in the bloodstream as an inactive zymogen. Upon activation by plasminogen activators such as tPA and uPA, PLG is converted into plasmin, which exhibits proteolytic activity essential for various physiological processes, including wound healing, tissue remodeling, and inflammation [1][2][3].
PLG interaction with various proteins, including those from pathogens is crucial for the immune response, as many pathogens exploit plasminogen to evade host defenses by binding to it and activating it to plasmin, which can degrade extracellular matrix components and promote tissue invasion [4][5][6]. In addition to its role in fibrinolysis, PLG is involved in cellular processes such as migration and invasion [7][8].
References:
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[2] N. Nguyen, F. Röttgerding, G. Devraj, Y. Lin, & P. Kraiczy, The complement binding and inhibitory protein cbia of borrelia miyamotoi degrades extracellular matrix components by interacting with plasmin(ogen), Frontiers in Cellular and Infection Microbiology, vol. 8, 2018. https://doi.org/10.3389/fcimb.2018.00023
[3] A. Rahi, A. Dhiman, D. Singh, A. Lynn, M. Rehan, & R. Bhatnagar, Exploring the interaction between mycobacterium tuberculosis enolase and human plasminogen using computational methods and experimental techniques, Journal of Cellular Biochemistry, vol. 119, no. 2, p. 2408-2417, 2017. https://doi.org/10.1002/jcb.26403
[4] A. Damm, Multifunctional interaction of cihc/fbpc orthologs of relapsing fever spirochetes with host-derived proteins involved in adhesion, fibrinolysis, and complement evasion, Frontiers in Immunology, vol. 15, 2024. https://doi.org/10.3389/fimmu.2024.1390468
[5] R. Nitzsche, J. Köhler, B. Kreikemeyer, & S. Oehmcke-Hecht, <b><i>streptococcus pyogenes</i></b> escapes killing from extracellular histones through plasminogen binding and activation by streptokinase, Journal of Innate Immunity, vol. 8, no. 6, p. 589-600, 2016. https://doi.org/10.1159/000448039
[6] S. Nguyen, B. Jovcevski, J. Truong, T. Pukala, & J. Bruning, A structural model of the human plasminogen and aspergillus fumigatus enolase complex, Proteins Structure Function and Bioinformatics, vol. 90, no. 8, p. 1509-1520, 2022. https://doi.org/10.1002/prot.26331
[7] S. Lighvani, N. Baik, J. Diggs, S. Khaldoyanidi, R. Parmer, & L. Miles, Regulation of macrophage migration by a novel plasminogen receptor plg-rkt, Blood, vol. 118, no. 20, p. 5622-5630, 2011. https://doi.org/10.1182/blood-2011-03-344242
[8] B. Thaler, N. Baik, P. Hohensinner, J. Baumgartner, A. Panzenböck, S. Stojkovićet al., Differential expression of plg-rkt and its effects on migration of proinflammatory monocyte and macrophage subsets, Blood, vol. 134, no. 6, p. 561-567, 2019. https://doi.org/10.1182/blood.2018850420
