Microginins are peptide protein phosphatase inhibitors initially produced by species of cyanobacteria Microcystis. Microginins inhibit zinc metalloproteinases such as leucine aminopeptidase and angiotensin-converting enzyme (ACE).
| Purity | ≥95% |
|---|---|
| Formula | C34H50N4O8S |
| Formula Wt. | 674.85 |
| Store Temp | -20°C |
|---|---|
| Ship Temp | Blue Ice |
| Info Sheet | M3207 Info Sheet PDF |
|---|
Schatz D, Keren Y, Vardi A, et al. Towards clarification of the biological role of microcystins, a family of cyanobacterial toxins. Environ Microbiol. 2007 Apr;9(4):965-70. PMID: 17359268.
Kraft M, Schleberger C, Weckesser J, et al. Binding structure of the leucine aminopeptidase inhibitor microginin FR1. FEBS Lett. 2006 Dec 22;580(30):6943-7. PMID: 17157838.
Runnage ME, Burke AJ, Davies SG, et al. Asymmetric Synthesis of the N-terminal component of Microginin: (2S,3R)-3-Amino-2-Hydroxydecanoic Acid, its (2R,3R)-Epimer and (3R)-3-Aminodecanoic Acid. Tetrahedron: Asymmetry. 1995;6(1):165-176.
matriks/Shikari® (S-ATP) Anti-Pembrolizumab ELISA w/confirmation/PEM-QNS-KEY
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goprolytix/Proteolytic Activation of Prothrombin/1 mg, 200 µg/BCT-DFP
novateinbio/Dynorphin A ( 13-17 ) Porcine Peptide/5mg/PE-54024_5mg
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