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| Product Name | ECE-1, Recombinant, Mouse (Endothelin Converting Enzyme-1) |
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| Description | Purity ≥90% (SDS-PAGE) under reducing conditions and visualized by silver stain Endotoxin: ≤1EU/ug (LAL). Endothelin-converting enzymes (ECEs) hydrolyze a specific peptide bond of big endothelins to produce active endothelins, some of the most potent vasoconstrictors known. ECE-1 is a member of the M13 zinc metallopeptidase family. Other members of the M13 family include thermolysin, neprilysin, Kell , and ECE-2. M13 metallopeptidases can be distinguished from other metallopeptidases by their sensitivity to inhibition by phosphoramidon. ECE-1 is most highly expressed in the cardiovascular endothelium, but is also expressed in some endocrine tissues. ECE-1 is known to hydrolyze a variety of bioactive pepti des, including bradykinin, neurotensin, angiotensins, and Substance P, with a substrate specificity similar to that of neprilysin. ECE-1 displays pronounced pH dependence in its substrate specificity. The degradation of Substance P by ECE-1 in endosomes regulates beta-arrestin-depend |
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| Size | 10ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | SwissProt: Q4PZA2 |
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| Catalog # | E3650-02 |
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| Order / More Info | ECE-1, Recombinant, Mouse (Endothelin Converting Enzyme-1) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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