Dynorphin A (1-10) TFA
CAS No.
Dynorphin A (1-10) TFA ( )
Catalog No. M30122 CAS No.
Dynorphin A (1-10) (TFA), an endogenous opioid neuropeptide, binds in the transmembrane domain of the κ-receptor.
Purity : >98% (HPLC)
COA
Datasheet
HNMR
HPLC
MSDS
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Biological Information
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Product NameDynorphin A (1-10) TFA
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NoteResearch use only, not for human use.
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Brief DescriptionDynorphin A (1-10) (TFA), an endogenous opioid neuropeptide, binds in the transmembrane domain of the κ-receptor.
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DescriptionDynorphin A (1-10) (TFA), an endogenous opioid neuropeptide, binds in the transmembrane domain of the κ-receptor.(In Vitro):Dynorphin A (1-10) (TFA), an endogenous opioid neuropeptide, binds in the transmembrane domain of the κ-receptor. The non-opioid actions of various forms of Dynorphin A (DynA) are examined on N-methyl-D-aspartate (NMDA) receptor channels in isolated rat trigeminal neurons using the whole-cell patch recording technique. All the dynorphins tested blocked NMDA-activated currents. The blocking actions are voltage-independent. The IC50 is 42.0 μM for DynA(1-10). To determine if shorter dynorphins have the similar blocking property, we examined the action of DynA(1-10) at different membrane potentials. DynA(1-10) blocks INMDA to a similar extent as the membrane potentials changed from -80 to +60 mV. Thus, despite a 160-fold difference in the apparent affinities, DynA(1-32) and DynA(1-10) both exert voltage-independent actions on NMDA receptors.
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Synonyms
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PathwayOthers
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TargetOther Targets
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Recptorκ-opioid receptor
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Research Area——
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Indication——
Chemical Information
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CAS Number--
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Formula Weight1348.5
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Molecular FormulaC59H92F3N19O14
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Purity>98% (HPLC)
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SolubilityH2O : 5 mg/mL (3.71 mM; Need ultrasonic)
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SMILES——
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Chemical Name
Shipping & Storage Information
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Storage(-20℃)
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ShippingWith Ice Pack
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Stability≥ 2 years
Reference
Paterlini G, et al. Molecular simulation of dynorphin A-(1-10) binding to extracellular loop 2 of the kappa-opioidreceptor. A model for receptor activation. J Med Chem. 1997 Sep 26;40(20):3254-62.
molnova catalog
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