Magainin 1 TFA (108433-99-4 free base)
CAS No.
Magainin 1 TFA (108433-99-4 free base)( )
Catalog No. M30276 CAS No.
Magainin 1 TFA is an antimicrobial amphiphilic peptide isolated from xenopus skin.
Magainin 1 TFA is an antimicrobial amphiphilic peptide isolated from xenopus skin.
Purity : >98% (HPLC)
COA
Datasheet
HNMR
HPLC
MSDS
Handing Instructions
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Biological Information
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Product NameMagainin 1 TFA (108433-99-4 free base)
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NoteResearch use only, not for human use.
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Brief DescriptionMagainin 1 TFA is an antimicrobial amphiphilic peptide isolated from xenopus skin.
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DescriptionMagainin 1 TFA is an antimicrobial amphiphilic peptide isolated from xenopus skin.(In Vitro):Magainin 1 interacts with acidic lipids through electrostatic interactions followed by hydrophobic interactions to form an amphiphilic helix, inducing the leakage. Magainin 1 induces the leakage of calcein specifically out of negatively-charged vesicles. The peptide binds to bovine brain phosphatidylserine sonicated vesicles according to the Langmuir isotherm with a binding constant of 3.8×105 M-1 and a binding-site number of 0.10 per lipid molecule.
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In Vitro
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In Vivo
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Synonyms
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PathwayOthers
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TargetOther Targets
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Recptor
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Research Area
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Indication
Chemical Information
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CAS Number--
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Formula Weight2523.87
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Molecular FormulaC114H178N29F3O30S
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Purity>98% (HPLC)
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Solubility
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SMILES
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Chemical NameSequence:Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-Gly-Lys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-Ile-Met-Lys-Ser
Shipping & Storage Information
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Storage(-20℃)
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ShippingWith Ice Pack
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Stability≥ 2 years
Reference
Duclohier H, et al. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys J. 1989 Nov;56(5):1017-21.
molnova catalog
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