tityustoxin kα tstx kα  (Alomone Labs)


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  • 86
    Name:
    Tityustoxin Kalpha
    Description:
    Tityustoxin Kalpha blocks cloned Kv1 2 with high potency
    Catalog Number:
    STT-360
    Price:
    274.0
    Category:
    Toxin
    Source:
    Synthetic peptide
    Applications:
    0
    Purity:
    >99% (HPLC)
    Size:
    0 1 mg
    Format:
    Lyophilized powder.
    Formula:
    C168H275N49O46S7
    Molecular Weight:
    3942 Da.
    Molecule Name:
    Tityustoxin-Kalpha, K+ channel toxin alpha-KTx 4.1, TsTX-K-alpha, TSK4, Toxin II-9
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    Structured Review

    Alomone Labs tityustoxin kα tstx kα
    Tityustoxin Kalpha
    Tityustoxin Kalpha blocks cloned Kv1 2 with high potency
    https://www.bioz.com/result/tityustoxin kα tstx kα/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tityustoxin kα tstx kα - by Bioz Stars, 2021-09
    86/100 stars

    Images

    1) Product Images from "Arrangement of Kv1 ? subunits dictates sensitivity to tetraethylammonium"

    Article Title: Arrangement of Kv1 ? subunits dictates sensitivity to tetraethylammonium

    Journal: The Journal of General Physiology

    doi: 10.1085/jgp.200910398

    Adjacently and diagonally arranged Kv1.1 and 1.2 tandem-linked gene constructs gave channels that were distinguished by TEA, but not AgTX1, TsTX-Kα, or KTX. (A) Current traces recorded using QPatch from an adjacent (Kv1.1-1.1-1.2-1.2) and diagonal (Kv1.2-1.1-1.2-1.1) channel in the absence (black) and presence of TEA, AgTX1, TsTX-Kα, or KTX (blue). (B) Dose–response curves for the forward and reverse adjacent channels show an ∼10-fold lower affinity for TEA than the corresponding diagonals. ○, Kv1.1-1.1-1.2-1.2; n = 5 cells for each concentration, manual patch clamp; Hill equation fit IC 50 = 9.6 mM, slope = 0.8. •, Kv1.2-1.2-1.1-1.1; Qpatch, n = 2–3; 8.2 mM, 0.6. □, Kv1.1-1.2-1.1-1.2; n = 4, Qpatch; 0.9 mM, 0.6. (blue) □, Kv1.1-1.2-1.1-1.2; n = 6–8, manual patch clamp; 1.1 mM, 0.6. ▪, Kv1.2-1.1-1.2-1.1; n = 3–5, Qpatch; 0.8 mM, 0.7. (Inset) Non-concatenated (red ▴; n = 6–7; 0.4 mM, 0.6) and concatenated (black ▴; n = 2–4; 0.7 mM, 0.7) homotetrameric Kv1.1 channels showed almost identical sensitivity to TEA, as with the less sensitive homotetrameric Kv1.2 (red ▾; n = 2–4; 41 mM, 0.6) channel and the tandem-linked homotetramer (black ▾; n = 3; 36 mM, 0.5). All homomer data were from Qpatch. (C) Channel dimers showed TEA susceptibilities similar to that for the pair of adjacently arranged tetrameric concatamers. □, Kv1.1-1.2; n = 8; 9.3 mM, 1.0. •, Kv1.2-1.1; n = 5–6; 7.8 mM, 0.7. ◆, Kv1.1-1.2 + Kv1.2-1.1; n = 9–11; 9.5 mM, 0.4. Data were from Qpatch. Error bars represent ± SEM.
    Figure Legend Snippet: Adjacently and diagonally arranged Kv1.1 and 1.2 tandem-linked gene constructs gave channels that were distinguished by TEA, but not AgTX1, TsTX-Kα, or KTX. (A) Current traces recorded using QPatch from an adjacent (Kv1.1-1.1-1.2-1.2) and diagonal (Kv1.2-1.1-1.2-1.1) channel in the absence (black) and presence of TEA, AgTX1, TsTX-Kα, or KTX (blue). (B) Dose–response curves for the forward and reverse adjacent channels show an ∼10-fold lower affinity for TEA than the corresponding diagonals. ○, Kv1.1-1.1-1.2-1.2; n = 5 cells for each concentration, manual patch clamp; Hill equation fit IC 50 = 9.6 mM, slope = 0.8. •, Kv1.2-1.2-1.1-1.1; Qpatch, n = 2–3; 8.2 mM, 0.6. □, Kv1.1-1.2-1.1-1.2; n = 4, Qpatch; 0.9 mM, 0.6. (blue) □, Kv1.1-1.2-1.1-1.2; n = 6–8, manual patch clamp; 1.1 mM, 0.6. ▪, Kv1.2-1.1-1.2-1.1; n = 3–5, Qpatch; 0.8 mM, 0.7. (Inset) Non-concatenated (red ▴; n = 6–7; 0.4 mM, 0.6) and concatenated (black ▴; n = 2–4; 0.7 mM, 0.7) homotetrameric Kv1.1 channels showed almost identical sensitivity to TEA, as with the less sensitive homotetrameric Kv1.2 (red ▾; n = 2–4; 41 mM, 0.6) channel and the tandem-linked homotetramer (black ▾; n = 3; 36 mM, 0.5). All homomer data were from Qpatch. (C) Channel dimers showed TEA susceptibilities similar to that for the pair of adjacently arranged tetrameric concatamers. □, Kv1.1-1.2; n = 8; 9.3 mM, 1.0. •, Kv1.2-1.1; n = 5–6; 7.8 mM, 0.7. ◆, Kv1.1-1.2 + Kv1.2-1.1; n = 9–11; 9.5 mM, 0.4. Data were from Qpatch. Error bars represent ± SEM.

    Techniques Used: Construct, Concentration Assay, Patch Clamp

    Recombinant Kv1 channels assembled on the surface of mammalian cells in active form. (A) Saturable binding (▾) of 125 I-αDTX to intact HEK-293 cells, expressing Kv1.1-1.1-1.2-1.2, quantified by a filtration assay. Relatively low values were recorded for nonsaturable (▴) binding compared with total (▪). Inset shows a Scatchard plot of the saturable binding. (B) Competition of 2.5 nM 125 I-αDTX binding to cells transfected (as in A) by αDTX, DTX k , or TsTx-Kα, which gave respective mean values for Ki of 0.6, 2.0, and 0.1 nM (error bars are ± SD; n = 4). (C) Antagonism of 2.5 nM 125 I-αDTX binding to cells expressing Kv1.1-1.1-1.2-1.2 (▪) or Kv1.2-1.1-1.2-1.1 (▴) channels by KTX gave respective IC 50 values of 12.4 ± 0.2 and 5.6 ± 0.1 nM (mean ± SD; n = 3).
    Figure Legend Snippet: Recombinant Kv1 channels assembled on the surface of mammalian cells in active form. (A) Saturable binding (▾) of 125 I-αDTX to intact HEK-293 cells, expressing Kv1.1-1.1-1.2-1.2, quantified by a filtration assay. Relatively low values were recorded for nonsaturable (▴) binding compared with total (▪). Inset shows a Scatchard plot of the saturable binding. (B) Competition of 2.5 nM 125 I-αDTX binding to cells transfected (as in A) by αDTX, DTX k , or TsTx-Kα, which gave respective mean values for Ki of 0.6, 2.0, and 0.1 nM (error bars are ± SD; n = 4). (C) Antagonism of 2.5 nM 125 I-αDTX binding to cells expressing Kv1.1-1.1-1.2-1.2 (▪) or Kv1.2-1.1-1.2-1.1 (▴) channels by KTX gave respective IC 50 values of 12.4 ± 0.2 and 5.6 ± 0.1 nM (mean ± SD; n = 3).

    Techniques Used: Recombinant, Binding Assay, Expressing, Filtration, Transfection

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    Alomone Labs tityustoxin kα tstx kα
    Adjacently and diagonally arranged Kv1.1 and 1.2 tandem-linked gene constructs gave channels that were distinguished by TEA, but not AgTX1, <t>TsTX-Kα,</t> or KTX. (A) Current traces recorded using QPatch from an adjacent (Kv1.1-1.1-1.2-1.2) and diagonal (Kv1.2-1.1-1.2-1.1) channel in the absence (black) and presence of TEA, AgTX1, TsTX-Kα, or KTX (blue). (B) Dose–response curves for the forward and reverse adjacent channels show an ∼10-fold lower affinity for TEA than the corresponding diagonals. ○, Kv1.1-1.1-1.2-1.2; n = 5 cells for each concentration, manual patch clamp; Hill equation fit IC 50 = 9.6 mM, slope = 0.8. •, Kv1.2-1.2-1.1-1.1; Qpatch, n = 2–3; 8.2 mM, 0.6. □, Kv1.1-1.2-1.1-1.2; n = 4, Qpatch; 0.9 mM, 0.6. (blue) □, Kv1.1-1.2-1.1-1.2; n = 6–8, manual patch clamp; 1.1 mM, 0.6. ▪, Kv1.2-1.1-1.2-1.1; n = 3–5, Qpatch; 0.8 mM, 0.7. (Inset) Non-concatenated (red ▴; n = 6–7; 0.4 mM, 0.6) and concatenated (black ▴; n = 2–4; 0.7 mM, 0.7) homotetrameric Kv1.1 channels showed almost identical sensitivity to TEA, as with the less sensitive homotetrameric Kv1.2 (red ▾; n = 2–4; 41 mM, 0.6) channel and the tandem-linked homotetramer (black ▾; n = 3; 36 mM, 0.5). All homomer data were from Qpatch. (C) Channel dimers showed TEA susceptibilities similar to that for the pair of adjacently arranged tetrameric concatamers. □, Kv1.1-1.2; n = 8; 9.3 mM, 1.0. •, Kv1.2-1.1; n = 5–6; 7.8 mM, 0.7. ◆, Kv1.1-1.2 + Kv1.2-1.1; n = 9–11; 9.5 mM, 0.4. Data were from Qpatch. Error bars represent ± SEM.
    Tityustoxin Kα Tstx Kα, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tityustoxin kα tstx kα/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tityustoxin kα tstx kα - by Bioz Stars, 2021-09
    86/100 stars
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    Adjacently and diagonally arranged Kv1.1 and 1.2 tandem-linked gene constructs gave channels that were distinguished by TEA, but not AgTX1, TsTX-Kα, or KTX. (A) Current traces recorded using QPatch from an adjacent (Kv1.1-1.1-1.2-1.2) and diagonal (Kv1.2-1.1-1.2-1.1) channel in the absence (black) and presence of TEA, AgTX1, TsTX-Kα, or KTX (blue). (B) Dose–response curves for the forward and reverse adjacent channels show an ∼10-fold lower affinity for TEA than the corresponding diagonals. ○, Kv1.1-1.1-1.2-1.2; n = 5 cells for each concentration, manual patch clamp; Hill equation fit IC 50 = 9.6 mM, slope = 0.8. •, Kv1.2-1.2-1.1-1.1; Qpatch, n = 2–3; 8.2 mM, 0.6. □, Kv1.1-1.2-1.1-1.2; n = 4, Qpatch; 0.9 mM, 0.6. (blue) □, Kv1.1-1.2-1.1-1.2; n = 6–8, manual patch clamp; 1.1 mM, 0.6. ▪, Kv1.2-1.1-1.2-1.1; n = 3–5, Qpatch; 0.8 mM, 0.7. (Inset) Non-concatenated (red ▴; n = 6–7; 0.4 mM, 0.6) and concatenated (black ▴; n = 2–4; 0.7 mM, 0.7) homotetrameric Kv1.1 channels showed almost identical sensitivity to TEA, as with the less sensitive homotetrameric Kv1.2 (red ▾; n = 2–4; 41 mM, 0.6) channel and the tandem-linked homotetramer (black ▾; n = 3; 36 mM, 0.5). All homomer data were from Qpatch. (C) Channel dimers showed TEA susceptibilities similar to that for the pair of adjacently arranged tetrameric concatamers. □, Kv1.1-1.2; n = 8; 9.3 mM, 1.0. •, Kv1.2-1.1; n = 5–6; 7.8 mM, 0.7. ◆, Kv1.1-1.2 + Kv1.2-1.1; n = 9–11; 9.5 mM, 0.4. Data were from Qpatch. Error bars represent ± SEM.

    Journal: The Journal of General Physiology

    Article Title: Arrangement of Kv1 ? subunits dictates sensitivity to tetraethylammonium

    doi: 10.1085/jgp.200910398

    Figure Lengend Snippet: Adjacently and diagonally arranged Kv1.1 and 1.2 tandem-linked gene constructs gave channels that were distinguished by TEA, but not AgTX1, TsTX-Kα, or KTX. (A) Current traces recorded using QPatch from an adjacent (Kv1.1-1.1-1.2-1.2) and diagonal (Kv1.2-1.1-1.2-1.1) channel in the absence (black) and presence of TEA, AgTX1, TsTX-Kα, or KTX (blue). (B) Dose–response curves for the forward and reverse adjacent channels show an ∼10-fold lower affinity for TEA than the corresponding diagonals. ○, Kv1.1-1.1-1.2-1.2; n = 5 cells for each concentration, manual patch clamp; Hill equation fit IC 50 = 9.6 mM, slope = 0.8. •, Kv1.2-1.2-1.1-1.1; Qpatch, n = 2–3; 8.2 mM, 0.6. □, Kv1.1-1.2-1.1-1.2; n = 4, Qpatch; 0.9 mM, 0.6. (blue) □, Kv1.1-1.2-1.1-1.2; n = 6–8, manual patch clamp; 1.1 mM, 0.6. ▪, Kv1.2-1.1-1.2-1.1; n = 3–5, Qpatch; 0.8 mM, 0.7. (Inset) Non-concatenated (red ▴; n = 6–7; 0.4 mM, 0.6) and concatenated (black ▴; n = 2–4; 0.7 mM, 0.7) homotetrameric Kv1.1 channels showed almost identical sensitivity to TEA, as with the less sensitive homotetrameric Kv1.2 (red ▾; n = 2–4; 41 mM, 0.6) channel and the tandem-linked homotetramer (black ▾; n = 3; 36 mM, 0.5). All homomer data were from Qpatch. (C) Channel dimers showed TEA susceptibilities similar to that for the pair of adjacently arranged tetrameric concatamers. □, Kv1.1-1.2; n = 8; 9.3 mM, 1.0. •, Kv1.2-1.1; n = 5–6; 7.8 mM, 0.7. ◆, Kv1.1-1.2 + Kv1.2-1.1; n = 9–11; 9.5 mM, 0.4. Data were from Qpatch. Error bars represent ± SEM.

    Article Snippet: Kaliotoxin (KTX), agitoxin-1 (AgTX1), and tityustoxin-Kα (TsTX-Kα) were purchased from Alomone Labs.

    Techniques: Construct, Concentration Assay, Patch Clamp

    Recombinant Kv1 channels assembled on the surface of mammalian cells in active form. (A) Saturable binding (▾) of 125 I-αDTX to intact HEK-293 cells, expressing Kv1.1-1.1-1.2-1.2, quantified by a filtration assay. Relatively low values were recorded for nonsaturable (▴) binding compared with total (▪). Inset shows a Scatchard plot of the saturable binding. (B) Competition of 2.5 nM 125 I-αDTX binding to cells transfected (as in A) by αDTX, DTX k , or TsTx-Kα, which gave respective mean values for Ki of 0.6, 2.0, and 0.1 nM (error bars are ± SD; n = 4). (C) Antagonism of 2.5 nM 125 I-αDTX binding to cells expressing Kv1.1-1.1-1.2-1.2 (▪) or Kv1.2-1.1-1.2-1.1 (▴) channels by KTX gave respective IC 50 values of 12.4 ± 0.2 and 5.6 ± 0.1 nM (mean ± SD; n = 3).

    Journal: The Journal of General Physiology

    Article Title: Arrangement of Kv1 ? subunits dictates sensitivity to tetraethylammonium

    doi: 10.1085/jgp.200910398

    Figure Lengend Snippet: Recombinant Kv1 channels assembled on the surface of mammalian cells in active form. (A) Saturable binding (▾) of 125 I-αDTX to intact HEK-293 cells, expressing Kv1.1-1.1-1.2-1.2, quantified by a filtration assay. Relatively low values were recorded for nonsaturable (▴) binding compared with total (▪). Inset shows a Scatchard plot of the saturable binding. (B) Competition of 2.5 nM 125 I-αDTX binding to cells transfected (as in A) by αDTX, DTX k , or TsTx-Kα, which gave respective mean values for Ki of 0.6, 2.0, and 0.1 nM (error bars are ± SD; n = 4). (C) Antagonism of 2.5 nM 125 I-αDTX binding to cells expressing Kv1.1-1.1-1.2-1.2 (▪) or Kv1.2-1.1-1.2-1.1 (▴) channels by KTX gave respective IC 50 values of 12.4 ± 0.2 and 5.6 ± 0.1 nM (mean ± SD; n = 3).

    Article Snippet: Kaliotoxin (KTX), agitoxin-1 (AgTX1), and tityustoxin-Kα (TsTX-Kα) were purchased from Alomone Labs.

    Techniques: Recombinant, Binding Assay, Expressing, Filtration, Transfection