Code | CSB-AP002261HU |
MSDS | |
Size | $142 |
Order now | |
Image | |
Have Questions? | Leave a Message or Start an on-line Chat |
The process of producing recombinant human Plasminogen protein (PLG) starts with the isolation of the gene encoding the PLG protein (98-356aa). This gene is cloned into an expression vector and introduced into E.coli cells. These cells are cultured in bioreactors to express the protein. After sufficient cell growth, the cells are lysed to release the protein, which is then purified using affinity chromatography. Rigorous quality control measures ensure the protein's purity and functionality before it is used in research applications. Its activity has been validated by an assay on anti-proliferation and anti-migration using endothelial cells in vitro and anti-angiogenesis in vivo, with a specific activity of 5.5x105 IU/mg. Its endotoxin content is less than 1.0 EU/μg as determined by the LAL method. Its purity is up to 95% as determined by SDS-PAGE.
PLG is a 92-kDa protein comprising 791 amino acids characterized by a serine protease region, five kringle domains, and an amino-terminal sequence [1]. Tissue plasminogen activator (t-PA) converts PLG into plasmin, an enzyme that degrades fibrin on clot surfaces. This conversion is enhanced when PLG binds to fibrin, increasing its affinity for t-PA [2]. Plasminogen receptors, including enolase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and phosphoglycerate kinase (PGK), are critical in microbial recruitment of plasminogen [3]. The protein interacts with various ligands through lysine binding sites within the five kringle domains at its N-terminus [4]. Besides its primary role in fibrin proteolysis, plasmin is also involved in cell migration, tissue remodeling, and inflammation [5]. Both plasminogen and Apo(a) contain kringle structural domains and a serine-proteinase region [6]. Furthermore, plasminogen-binding proteins that expose C-terminal basic residues on cell surfaces predominantly enhance plasminogen activation [7]. Pathogens bind plasminogen to their surface, activating plasmin to degrade the host extracellular matrix [8]. Enolase-expressing pathogens, including plasmodium, bind to plasminogen, helping pathogen adhesion and extracellular matrix degradation [9].
References:
[1] T. Dejouvencel, L. Doeuvre, R. Lacroix, P. Laurent, F. Dignat-George, H. Lijnenet al., Fibrinolytic cross-talk: a new mechanism for plasmin formation, Blood, vol. 115, no. 10, p. 2048-2056, 2010. https://doi.org/10.1182/blood-2009-06-228817
[2] E. Nilebäck, F. Westberg, J. Deinum, & S. Svedhem, Viscoelastic sensing of conformational changes in plasminogen induced upon binding of low molecular weight compounds, Analytical Chemistry, vol. 82, no. 20, p. 8374-8376, 2010. https://doi.org/10.1021/ac1016419
[3] J. Stie, G. Bruni, & D. Fox, Surface-associated plasminogen binding of cryptococcus neoformans promotes extracellular matrix invasion, Plos One, vol. 4, no. 6, p. e5780, 2009. https://doi.org/10.1371/journal.pone.0005780
[4] M. Sanderson-Smith, M. Dowton, M. Ranson, & M. Walker, The plasminogen-binding group a streptococcal m protein-related protein prp binds plasminogen via arginine and histidine residues, Journal of Bacteriology, vol. 189, no. 4, p. 1435-1440, 2007. https://doi.org/10.1128/jb.01218-06
[5] E. Plow, D. Freaney, J. Plescia, & L. Miles, The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type., The Journal of Cell Biology, vol. 103, no. 6, p. 2411-2420, 1986. https://doi.org/10.1083/jcb.103.6.2411
[6] E. Anglés-Cano, A. Díaz, & S. Loyau, Inhibition of fibrinolysis by lipoprotein(a), Annals of the New York Academy of Sciences, vol. 936, no. 1, p. 261-275, 2001. https://doi.org/10.1111/j.1749-6632.2001.tb03514.x
[7] N. Andronicos, E. Chen, N. Baik, H. Bai, C. Parmer, W. Kiosseset al., Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, plg-rkt, a major regulator of cell surface plasminogen activation, Blood, vol. 115, no. 7, p. 1319-1330, 2010. https://doi.org/10.1182/blood-2008-11-188938
[8] S. Poltermann, A. Kunert, M. Heide, R. Eck, A. Hartmann, & P. Zipfel, Gpm1p is a factor h-, fhl-1-, and plasminogen-binding surface protein of candida albicans, Journal of Biological Chemistry, vol. 282, no. 52, p. 37537-37544, 2007. https://doi.org/10.1074/jbc.m707280200
[9] A. Ghosh and M. Jacobs-Lorena, Surface-expressed enolases of plasmodium and other pathogens, Memórias Do Instituto Oswaldo Cruz, vol. 106, no. suppl 1, p. 85-90, 2011. https://doi.org/10.1590/s0074-02762011000900011
There are currently no reviews for this product.