Human Neurotrophin 3 Protein (RMPP-00230362)
Cat. No.: RMPP-00230362
Category: Native Protein
Research Area: Cardiovascular
INQUIRY
10 μg
Customer Size
Product Features
| Source | Native |
|---|---|
| Purity | > 95% SDS-PAGE. |
| Nature | Native |
| Animal Free | No |
| Form | Liquid |
| Applications | Functional Studies; SDS-PAGE |
| Key Features | Expression system: Native; Purity: > 95% SDS-PAGE; Active: Yes; Suitable for: Functional Studies, SDS-PAGE |
Protein Information
| UniProt ID | P07204 |
|---|---|
| Sequence Similarities | Contains 1 C-type lectin domain. Contains 6 EGF-like domains. |
| Protein Length | Full length protein |
| Cellular Localization | Membrane. |
| Tissue Specificity | Endothelial cells are unique in synthesizing thrombomodulin. |
| Function | Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated. |
| Involvement in Disease | Defects in THBD are the cause of thrombophilia due to thrombomodulin defect (THR-THBD). A hemostatic disorder characterized by a tendency to thrombosis.Defects in THBD are a cause of susceptibility to hemolytic uremic syndrome atypical type 6 (AHUS6). An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. |
| Post-translational Modifications | N-glycosylated.The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. |
Storage & Shipping
| Shipping and Storage | Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles. pH: 7.40Preservative: 0.02% Sodium azideConstituents: 0.242% Tris, 0.87% Sodium chloride This product is an active protein and may elicit a biological response in vivo, handle with caution. |
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For research use only. Not for clinical use.
