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| Size | 100ug |
|---|---|
| Brand | Arovia |
| Product type | Recombinant Proteins |
| Product name | Recombinant Human CD201/PROCR, N-His |
|---|---|
| Origin species | Human |
| Expression system | Prokaryotic expression |
| Molecular weight | 24.33 kDa |
| Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Form | Liquid |
| Delivery condition | Dry Ice |
| Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
| Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
| Brand | Arovia |
| Host species | Escherichia coli (E.coli) |
| Fragment Type | Ser18-Ser210 |
| Aliases /Synonyms | Endothelial protein C receptor, PROCR, EPCR, APC receptor, Endothelial cell protein C receptor, CD201, Activated protein C receptor |
| Reference | ARO-P13001 |
| Note | For research use only. |
Recombinant Human CD201, also known as PROCR, is a protein that plays a crucial role in the regulation of blood coagulation and inflammation. It is a transmembrane glycoprotein that is expressed on the surface of endothelial cells and acts as a receptor for the anticoagulant protein C. In this article, we will explore the structure, activity, and applications of Recombinant Human CD201/PROCR.
Recombinant Human CD201/PROCR is a 72 kDa protein consisting of 484 amino acids. It is composed of an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The extracellular domain contains two epidermal growth factor (EGF)-like domains and six tandemly repeated sushi domains. These domains are responsible for the binding of protein C and other ligands. The transmembrane domain anchors the protein to the cell membrane, while the cytoplasmic domain is involved in intracellular signaling.
The main function of Recombinant Human CD201/PROCR is to enhance the activity of protein C, a natural anticoagulant, by facilitating its activation. This is achieved through the binding of protein C to the EGF-like domains of CD201/PROCR, which triggers a conformational change in protein C and exposes its active site. Activated protein C then inhibits the coagulation cascade by inactivating factors Va and VIIIa. This activity of CD201/PROCR is essential for maintaining the balance between coagulation and anticoagulation in the body.
In addition to its anticoagulant activity, CD201/PROCR also has anti-inflammatory properties. It has been shown to inhibit the production of pro-inflammatory cytokines and chemokines, and to promote the production of anti-inflammatory molecules. This makes CD201/PROCR an important regulator of the inflammatory response in various diseases.
Recombinant Human CD201/PROCR has a wide range of potential applications in the field of medicine. One of the most significant applications is in the treatment of thrombotic disorders. Mutations in the gene encoding CD201/PROCR have been associated with an increased risk of thrombosis. Recombinant Human CD201/PROCR can be used as a therapeutic agent to restore the balance between coagulation and anticoagulation in these patients.
Another potential application of Recombinant Human CD201/PROCR is in the treatment of inflammatory diseases. As mentioned earlier, CD201/PROCR has anti-inflammatory properties, which make it a promising target for the development of novel anti-inflammatory drugs. Recombinant Human CD201/PROCR can also be used in combination with other anti-inflammatory agents to enhance their effectiveness.
Moreover, Recombinant Human CD201/PROCR has been studied for its potential role in cancer therapy. It has been shown to inhibit the growth and metastasis of certain types of cancer cells, making it a potential target for the development of anti-cancer drugs.
In summary, Recombinant Human CD201/PROCR is a multifunctional protein with important roles in blood coagulation and inflammation. Its structure, activity, and potential applications make it a promising therapeutic target for various diseases. Further research on this protein will help us better understand its function and explore its potential in the development of new treatments for a variety of medical conditions.
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