Active Recombinant Human PLG Protein, Fc Chimera
Cat.No. : | PLG-1107H |
Product Overview : | Recombinant Human PLG (Accession # P00747), fused with , was produced in Mouse myeloma cell line, NS0-derived. |
- Specification
- Gene Information
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Source : | Mammalian cells |
Species : | Human |
Tag : | Fc |
Predicted N Terminal : | Met-Asp-Pro100 |
Form : | Lyophilized from a 0.2 µm filtered solution in PBS. |
Bio-activity : | Measured by the ability of the immobilized protein to support the adhesion of THP-1 human acute monocytic leukemia cells. Chavakis, T. et al. (2005) Blood 10^5:1036.The ED50 for this effect is typically 0.5-2.5 µg/mL. |
Molecular Mass : | Recombinant Human PLG, Fc Chimera has a calculated MW of 67.7 kDa (monomer). In SDS-PAGE migrates as 75-85 kDa, reducing conditions. |
Purity : | >95%, by SDS-PAGE with silver staining, under reducing conditions. |
Storage : | Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: In lyophilized state for 1 year (4ºC); After reconstitution under sterile conditions for 3 months (-70ºC). |
Gene Name : | PLG plasminogen [ Homo sapiens ] |
Official Symbol : | PLG |
Synonyms : | PLG; plasminogen; plasmin; DKFZp779M0222; |
Gene ID : | 5340 |
mRNA Refseq : | NM_001168338 |
Protein Refseq : | NP_001161810 |
MIM : | 173350 |
UniProt ID : | P00747 |
Chromosome Location : | 6q26 |
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PLG-6846M | Recombinant Mouse PLG Protein, His (Fc)-Avi-tagged | +Inquiry |
◆ Native Protein | ||
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◆ Lysates | ||
PLG-3109HCL | Recombinant Human PLG 293 Cell Lysate | +Inquiry |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (7)
Ask a questionPLG has been investigated as a potential diagnostic and prognostic biomarker for various diseases. For instance, altered PLG levels have been observed in cancer patients, serving as a potential marker for tumor progression and prognosis. Additionally, PLG has been implicated in cardiovascular diseases, where its levels can reflect the severity of certain conditions, such as thrombosis. Moreover, PLG may have utility as a biomarker in inflammatory disorders and neurological diseases. Further research is needed to validate the clinical utility of PLG as a biomarker and develop specific assays for its detection.
Dysregulation of PLG has been associated with several pathological conditions. Decreased PLG levels or impaired activation can lead to impaired fibrinolysis, resulting in the formation of excessive blood clots. On the other hand, increased PLG activation or excessive Plasmin activity can promote tissue degradation, contributing to diseases such as chronic inflammation, cancer metastasis, and tissue damage. Moreover, PLG has been implicated in the pathogenesis of neurodegenerative disorders and cardiovascular diseases. Understanding the mechanisms underlying PLG dysregulation is crucial for designing therapeutic strategies to counteract its pathological implications.
PLG-targeted therapeutic strategies have shown promise in various diseases. For example, agents that enhance PLG activation, such as tPA and uPA, have been employed to promote fibrinolysis and dissolve blood clots in conditions such as heart attacks and ischemic strokes. Conversely, inhibitors of PLG activation, such as PAIs, can be used to prevent excessive fibrinolysis and subsequent bleeding complications. Additionally, targeting PLG receptors or manipulating PLG interactions with other molecules may offer potential therapeutic avenues. However, further research is required to optimize these strategies and assess their efficacy and safety in clinical settings.
The PLG protein, also known as Plasminogen, is a single-chain glycoprotein composed of 790 amino acids. It consists of several domains, including a signal peptide, five kringle domains (K1-K5), and a serine protease domain. The signal peptide mediates protein secretion, while the kringle domains have numerous functions, such as binding to receptors and ligands. The serine protease domain is responsible for the conversion of Plasminogen to active Plasmin, a crucial enzyme in fibrinolysis and extracellular matrix remodeling processes.
PLG plays a vital role in several physiological processes. Its primary function is as a precursor to Plasmin, which is involved in the degradation of blood clots (fibrinolysis). Plasmin also participates in tissue remodeling, wound healing, and cell migration. Additionally, PLG has been implicated in immune responses, angiogenesis, and cell adhesion. Its ability to interact with various receptors and bind to components of the extracellular matrix highlights its diverse and important functions in maintaining normal physiological homeostasis.
PLG, also known as plasminogen, plays a crucial role in the fibrinolytic system. Its main biological function is to be converted into plasmin, an enzyme that breaks down fibrin clots. Plasminogen is activated by tissue plasminogen activator (tPA), which cleaves it into active plasmin. Plasmin then degrades fibrin clots, preventing the formation of thrombi and promoting the dissolution of existing blood clots. Additionally, PLG is involved in various physiological processes, such as wound healing, tissue remodeling, cell migration, and inflammation.
The activation of PLG is tightly regulated to prevent undesired fibrinolysis. Activation can occur through two main pathways: the tissue-type Plasminogen Activator (tPA)-dependent pathway and the urokinase-type Plasminogen Activator (uPA)-dependent pathway. In the tPA-dependent pathway, tPA binds to a specific receptor on the cell surface and catalyzes the conversion of PLG to Plasmin. The uPA-dependent pathway involves uPA binding to a receptor, followed by the activation of PLG. Additionally, various regulatory proteins, such as Plasminogen Activator Inhibitors (PAIs), control PLG activation by inhibiting the activity of tPA and uPA.
Customer Reviews (3)
Write a reviewThe tightly sealed packaging of this protein reagent ensures optimal preservation of its activity.
I highly recommend this reagent for its simplified experimental workflow, saving time and experimental costs.
Catering to diverse experimental needs, its outstanding performance facilitates diversity in scientific research.
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