Mittx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
Average 93 stars, based on 3 article reviews
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1) Product Images from "Structure and analysis of nanobody binding to the human ASIC1a ion channel"
Article Title: Structure and analysis of nanobody binding to the human ASIC1a ion channel
Figure Legend Snippet: Effects of Nb.C1 on MitTx and PcTx1 binding to hASIC1a. ( A ) Representative currents of an oocyte expressing hASIC1a activated with pH 6.0 followed by a second activation with 50 nM MitTx at pH 7.4. ( B ) Same experiment after pre-incubation of the oocyte with 50 nM Nb.C1 for 15 min. ( C ) Summary of the peak currents from pH 6.0 and MitTx activations. In this and all traces, the conditioning pH is 7.4. The bars represent the mean±SD of currents, n=8 Nb control and n=6 Nb.C1. Asterisks indicate statistical significance in t-test, p
Techniques Used: Binding Assay, Expressing, Activation Assay, Incubation
Figure Legend Snippet: Structural comparison of hASIC1a-Nb.C1 complex to toxin-bound ASICs. Two side, top and bottom views of superimposed structures of hASIC1a-NbC1 complex (red) with ( A ) MitTx-bound to chicken ASIC1 (4ntw) in open conformation (orange). In side views, the threefold axis of the channel is indicated by a dashed vertical line; in top and bottom views it is indicated by dotted triangles. ( B ) PcTx1-bound chicken ASIC1 (3s3x) (gray). ( C ) Mambalgin-1-bound human ASIC1 (7ctf) (blue). Only one subunit is shown for simplicity. Surface clashes are indicated by dashed rectangles. Nb.C1, MitTx- α, MitTx- β, PcTx1, Mambalgin-1 are shown as red, orange, light-orange, light-purple, marine respectively.
2) Product Images from "Epithelial Sodium Channel-α Mediates the Protective Effect of the TNF-Derived TIP Peptide in Pneumolysin-Induced Endothelial Barrier Dysfunction"
Article Title: Epithelial Sodium Channel-α Mediates the Protective Effect of the TNF-Derived TIP Peptide in Pneumolysin-Induced Endothelial Barrier Dysfunction
Journal: Frontiers in Immunology
Figure Legend Snippet: Proposed sequence of events in the role of epithelial sodium channel (ENaC)-α in barrier protection in pneumolysin (PLY)-treated human lung microvascular endothelial cells. PLY, upon pore formation, increases Ca 2+ -influx ( 3 ), which in turn mobilizes calmodulin. Calmodulin activates CaMKII, which in turn phosphorylates its substrate filamin A (FLN-A) ( 15 ). Phosphorylated FLN-A promotes stress fiber formation and increases capillary permeability. Activation of NSC, by either TIP peptide (binding to ENaC-α) or MitTx [binding to acid-sensing ion channel 1a (ASIC1a)], abrogates PLY-mediated CaMKII activation and protects as such from PLY-induced hyperpermeability.
Techniques Used: Sequencing, Permeability, Activation Assay, Binding Assay