Recombinant Human Plasminogen Protein

Beta LifeScience SKU/CAT #: BLA-7099P

Recombinant Human Plasminogen Protein

Beta LifeScience SKU/CAT #: BLA-7099P
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Product Overview

Host Species Human
Accession P00747
Synonym Plasmin Plasmin heavy chain A Plasmin light chain B Plasminogen PLG PLMN_HUMAN
Description Recombinant Human Plasminogen Protein was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 30 kDa
Purity >95% SDS-PAGE.>95% HPLC analyses.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Fully biologically active when compared to standard. The activity is assayed onanti-proliferation and anti-migration of endothelial cells in vitro and antiangiogenesisin vivo. The specific activity of anti-migration of endothelial cells invitro is 0.55x105Units/mg.
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C. Avoid freeze / thaw cycle.

Target Details

Target Function Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.; Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Subcellular Location Secreted. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.
Protein Families Peptidase S1 family, Plasminogen subfamily
Database References
Associated Diseases Plasminogen deficiency (PLGD)
Tissue Specificity Present in plasma and many other extracellular fluids. It is synthesized in the liver.

Gene Functions References

  1. Apo(a) attenuates cell-surface plasmin-mediated conversion of Glu- to Lys-plasminogen. PMID: 29990619
  2. Urinary angiostatin and VCAM-1 are predictive of specific histological changes in concurrent lupus nephritis renal biopsies. PMID: 29076253
  3. We did not find an association of the AgP risk variant rs4252120 with CP. However, we identified a haplotype block downstream of PLG, which showed shared association with CP and AgP. PMID: 28548211
  4. The homozygous alleles in F12 (rs1801020) and F13 (rs5985) was identified a genetic risk profile of thromboembolism in a Family. PMID: 27976734
  5. Our findings that plasminogen and pSTAT3 are significantly associated with LI suggest that they may represent signaling nodes or biomarkers of pathways common to the processes of postlactational involution and LI. PMID: 28752190
  6. A rare non-conservative missense mutation was newly identified in exon 9 of the PLG gene. PMID: 29548426
  7. Plasminogen binds to the cell surface-exposed proteins of Candida parapsilosis. PMID: 28651026
  8. plasmin cleaves surface-bound CCL21 to release the C-terminal peptide responsible for CCL21 binding to glycosaminoglycans on the extracellular matrix and cell surfaces, thereby generating the soluble form. PMID: 27301418
  9. Analysis of plasminogen genetic variants in multiple sclerosis patients has been reported. PMID: 27194806
  10. Enolase of Mtb is present on its surface and binds human plasminogen with high affinity. PMID: 27569900
  11. The mechanism for plasminogen/M protein binding uncovered here may facilitate targeting of group A Streptococcus pyogenes virulence factors for disease management PMID: 28724633
  12. t-PA binds to Lys91 in the MBP NH2-terminal region and PLG binds to Lys122 in the MBP COOH-terminal region. This proximity promotes the activation of PLG by t-PA. PMID: 28648598
  13. in the presence of platelet polyphosphate and the downstream substrate fibrin, alphaFXIIa is a highly efficient and favorable plasminogen activator. PMID: 27694320
  14. Plasmin(ogen) serves as a favorable biomarker for prediction of survival in advanced high-grade serous ovarian cancer PMID: 27935848
  15. Our findings indicate a new pathway for bradykinin formation in patients with HAE, in which FXII is cleaved and activated by plasmin. PMID: 27130860
  16. VWF susceptibility to plasmin proteolysis at K1491-R1492 is modulated by local N-linked glycan expression within A1A2A3, and specifically inhibited by heparin binding to the A1 domain. PMID: 28279966
  17. bone morphogenetic proteins (BMPs) and mature BMPs that have been further cleaved by serum proteases induce cell cycle entry by dedifferentiating newt muscle cells. PMID: 28350991
  18. Plasminogen and P4HA2 are involved in vascular remodelling and angiogenesis, suggesting a high relevance of these processes for the pathogenic mechanisms underlying this type of vasculitis PMID: 28041642
  19. Plasminogen and OxPL-PLG were lower in patients presenting with an acute MI than in those with stable CAD and also in those with atherothrombotic MI (Type 1) vs. those with non-atherothrombotic MI (Type 2). PMID: 26510751
  20. Although carriers with PLG:p.Ala620Thr show low plasminogen activity, this is not a predisposing variant for aHUS; and individuals of dysplasminogenemia are not at significantly increased risk of aHUS. PMID: 27194432
  21. Five novel plasminogen gene mutations have been found in Turkish patients with type I plasminogen deficiency. PMID: 26340456
  22. A novel plasminogen gene mutation, deficiency of plasminogen antigen and activity, and anti-plasminogen IgG and IgA antibodies were identified in a patient with adult-onset ligneous conjunctivitis. PMID: 25674820
  23. S. aureus NCTC 8325-4 adheres to immobilized plasminogen in vitro and that the adhesion may be mediated by a C-terminal fragment of the PBP3 protein.[PBP3] PMID: 27488131
  24. we demonstrated that PLG functions as a molecular bridge between tricellulin and streptococcal surface enolase (SEN). The wild type strain efficiently translocated across the epithelial monolayer, accompanied by cleavage of transmembrane junctional proteins. PMID: 26822058
  25. Suggest that tubulointerstitial plasmin is associated with inflammation leading to renal fibrosis, and can cause the decline in renal function seen in patients with IgA nephropathy. PMID: 25971850
  26. Plasminogen binding and activation by different glycolytic enzymes of M. pneumoniae play a role in successful colonization of the human respiratory tract. PMID: 26667841
  27. reduced proteolytic activity of plasmin on structures of growing thrombi, rather than on complement activation fragments, explains the association of plasminogen deficiency with aHUS. PMID: 26637181
  28. Zinc modulates fibrinolysis by attenuating tPA-mediated plasminogen activation and plasmin-induced fibrin degradation. PMID: 25789495
  29. These results indicate that FXIIIa activity can be modulated by fibrinolytic enzymes, and suggest that changes in fibrinolytic activity may influence cross-linking of blood proteins. PMID: 26359437
  30. Plasmin cleavage of iC3b provides a complement regulatory pathway that is as efficient as FI/CR1 but does not require a cellular cofactor. PMID: 25556624
  31. PLG is the third replicated shared genetic risk factor of atherosclerosis and periodontitis. PMID: 25466412
  32. Data show that preincubation with plasminogen, wild-type group A Streptococcus (GAS) NS88.2 degraded complement C3b. PMID: 23969887
  33. whereas the presence of plasminogen did not affect the factor I cofactor activity of C4BP, the activation of plasminogen by urokinase-type plasminogen activator to active plasmin was significantly augmented in the presence of C4BP. PMID: 26067271
  34. These studies demonstrate that GAS virulence can be explained by disparate hPg activation by SK2a and SK2b coupled with the coinherited M-proteins of these strains PMID: 26070561
  35. PAM activated Plasminogen Glycoform II. PMID: 26029848
  36. High plasma fibrinogen and low plasminogen are associated with poor survival in CTEPH patients without modern therapy. PMID: 24909805
  37. Data show that different subpopulations of platelets harbor plasminogen by diverse mechanisms PMID: 25712989
  38. manganese transport protein C (MntC) is an extracellular matrix- and plasminogen-binding protein PMID: 25409527
  39. This review highlights the importance of the best-characterized components of the PLG/PLA cascade in the pathogenesis of cancer focusing on the role of the cell surface-PLG receptors (PLG-R). [review] PMID: 25407528
  40. IGF-II, TGF-beta1 and VEGF-A and its receptor in malignant tumor tissue, as well as increasedplasmin release from proenzyme and MMP-3 activationis apparently associated with the formation of pathogenic mechanism of vasculature development PMID: 25993872
  41. Angiostatin may play a role in the pathophysiology of preeclampsia. PMID: 24205998
  42. The results suggested that EF-Tu and Eno serve as surface receptors for B. longum NCC2705 binding to human plasminogen. PMID: 24840471
  43. Human plasmin activity loss results from the C-terminal lysine-dependent redistribution of enzyme molecules on a fibrin surface. PMID: 25222106
  44. Genome-wide association analyses revealed common DNA variants in PLG, LPA, and near SIGLEC14 that contribute to plasma plasminogen level variation. PMID: 25208887
  45. ANG interacts with plasminogen activation system at the leading edges of breast cancer cell surfaces and facilitates interactions of uPAR with uPA to regulate plasmin formation and cell migration. PMID: 24457100
  46. Reduced plasminogen binding and delayed activation render gamma'-fibrin more resistant to lysis than gammaA-fibrin. PMID: 25128532
  47. Binding of streptokinase Lys(414) to plasminogen kringle 4 plays a role in recognition of plasminogen by streptokinase. PMID: 25138220
  48. The surface-displayed enolase, which serves as major pneumococcal plasminogen receptor, was identified as a key factor for plasminogen-mediated bacterial attachment in infection analyses with Streptococcus pneumoniae. PMID: 23906818
  49. The results demonstrate that Bacteroides fragilis Bfp60 surface adhesin is responsible for the recognition of laminin and plasminogen-plasmin activation. PMID: 23850366
  50. We propose that plasminogen activation on endothelial cells acts as a natural backup for ADAMTS13 to degrade obstructive platelet-VWF complexes. PMID: 24449821


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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