latrotoxin  (Alomone Labs)


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    Structured Review

    Alomone Labs latrotoxin
    sNG2 + cells and hilar interneurons do not respond to the same excitatory synapses, despite their close spatial association A. Example of mEPSC activity recorded in a hilar EGFP + interneuron (upper panel, upper trace) and its sNG2 + cell (upper panel, lower trace) in the presence of 1 μM TTX. By applying 0.3 nM <t>latrotoxin</t> for 5 minutes and then switching to a 0.5 mM Ca ++ solution, we were able to induce bursts of mEPSCs both in the interneuron (b1, lower panel, upper trace) and in its sNG2 + cell (b2, lower panel, lower trace). B. Cross-correlation histogram shows the absence of non-random synchronized mEPSCs in closely associated pairs of EGFP + interneurons and sNG2 + cells. The histogram shows data pooled from 8 NG2 + cell/interneuron pairs. All recordings were performed in the presence of 100 μM picrotoxin using a Cesium/methanesulfonate internal solution.
    Latrotoxin, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    latrotoxin - by Bioz Stars, 2022-12
    92/100 stars

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    1) Product Images from "Satellite NG2 progenitor cells share common glutamatergic inputs with associated interneurons in the mouse dentate gyrus"

    Article Title: Satellite NG2 progenitor cells share common glutamatergic inputs with associated interneurons in the mouse dentate gyrus

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.1355-08.2008

    sNG2 + cells and hilar interneurons do not respond to the same excitatory synapses, despite their close spatial association A. Example of mEPSC activity recorded in a hilar EGFP + interneuron (upper panel, upper trace) and its sNG2 + cell (upper panel, lower trace) in the presence of 1 μM TTX. By applying 0.3 nM latrotoxin for 5 minutes and then switching to a 0.5 mM Ca ++ solution, we were able to induce bursts of mEPSCs both in the interneuron (b1, lower panel, upper trace) and in its sNG2 + cell (b2, lower panel, lower trace). B. Cross-correlation histogram shows the absence of non-random synchronized mEPSCs in closely associated pairs of EGFP + interneurons and sNG2 + cells. The histogram shows data pooled from 8 NG2 + cell/interneuron pairs. All recordings were performed in the presence of 100 μM picrotoxin using a Cesium/methanesulfonate internal solution.
    Figure Legend Snippet: sNG2 + cells and hilar interneurons do not respond to the same excitatory synapses, despite their close spatial association A. Example of mEPSC activity recorded in a hilar EGFP + interneuron (upper panel, upper trace) and its sNG2 + cell (upper panel, lower trace) in the presence of 1 μM TTX. By applying 0.3 nM latrotoxin for 5 minutes and then switching to a 0.5 mM Ca ++ solution, we were able to induce bursts of mEPSCs both in the interneuron (b1, lower panel, upper trace) and in its sNG2 + cell (b2, lower panel, lower trace). B. Cross-correlation histogram shows the absence of non-random synchronized mEPSCs in closely associated pairs of EGFP + interneurons and sNG2 + cells. The histogram shows data pooled from 8 NG2 + cell/interneuron pairs. All recordings were performed in the presence of 100 μM picrotoxin using a Cesium/methanesulfonate internal solution.

    Techniques Used: Activity Assay

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    Alomone Labs native α ltx
    Monoclonal scFv ELISA signals against <t>α-LTX.</t> In total, 534 scFv clones were expressed in solution and screened for their ability to bind directly coated α-LTX. scFvs displaying a binding signal above the cut-off absorbance value of 0.5 (dotted line) at 492 nm were considered hits.
    Native α Ltx, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    native α ltx - by Bioz Stars, 2022-12
    92/100 stars
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    Monoclonal scFv ELISA signals against α-LTX. In total, 534 scFv clones were expressed in solution and screened for their ability to bind directly coated α-LTX. scFvs displaying a binding signal above the cut-off absorbance value of 0.5 (dotted line) at 492 nm were considered hits.

    Journal: Frontiers in Immunology

    Article Title: Discovery of a Recombinant Human Monoclonal Immunoglobulin G Antibody Against α-Latrotoxin From the Mediterranean Black Widow Spider (Latrodectus tredecimguttatus)

    doi: 10.3389/fimmu.2020.587825

    Figure Lengend Snippet: Monoclonal scFv ELISA signals against α-LTX. In total, 534 scFv clones were expressed in solution and screened for their ability to bind directly coated α-LTX. scFvs displaying a binding signal above the cut-off absorbance value of 0.5 (dotted line) at 492 nm were considered hits.

    Article Snippet: ReagentsLyophilized native α-LTX ( > 98% purity) was obtained from Alomone Labs (Jerusalem, Israel, LSP-130).

    Techniques: Enzyme-linked Immunosorbent Assay, Clone Assay, Binding Assay

    Output and assessment of phage display selections against α-LTX. (A) Accumulation of scFv-displaying phages from the IONTAS phage display library λ with affinity to α-LTX over three rounds of selection. An increase in CFU/ml of 375-fold and 22-fold respectively were observed between the selection rounds. (B) CFU/ml was determined for output phages from selection round two and three for binding to either α-LTX, streptavidin, or milk proteins. An increase of 30-fold between the second and third selection round was observed in CFU/ml for the phages that bound streptavidin-captured α-LTX. Only few phages with affinity to streptavidin or milk proteins were accumulated compared to phages with affinity to α-LTX.

    Journal: Frontiers in Immunology

    Article Title: Discovery of a Recombinant Human Monoclonal Immunoglobulin G Antibody Against α-Latrotoxin From the Mediterranean Black Widow Spider (Latrodectus tredecimguttatus)

    doi: 10.3389/fimmu.2020.587825

    Figure Lengend Snippet: Output and assessment of phage display selections against α-LTX. (A) Accumulation of scFv-displaying phages from the IONTAS phage display library λ with affinity to α-LTX over three rounds of selection. An increase in CFU/ml of 375-fold and 22-fold respectively were observed between the selection rounds. (B) CFU/ml was determined for output phages from selection round two and three for binding to either α-LTX, streptavidin, or milk proteins. An increase of 30-fold between the second and third selection round was observed in CFU/ml for the phages that bound streptavidin-captured α-LTX. Only few phages with affinity to streptavidin or milk proteins were accumulated compared to phages with affinity to α-LTX.

    Article Snippet: ReagentsLyophilized native α-LTX ( > 98% purity) was obtained from Alomone Labs (Jerusalem, Israel, LSP-130).

    Techniques: Selection, Binding Assay

    Monoclonal IgG ELISA signals against (A) α-LTX and (B) L. tredecimguttatus whole venom. The binding capability of TPL0020_02_G9 to α-LTX was assessed using different concentrations of IgG. The binding specificity was evaluated by testing the binding of the IgG to three controls (binding to milk proteins, streptavidin, and neutravidin) using the highest IgG concentration (2,000 ng/ml). Each column represents the average of triplicate measurements with error bars indicating the standard deviation.

    Journal: Frontiers in Immunology

    Article Title: Discovery of a Recombinant Human Monoclonal Immunoglobulin G Antibody Against α-Latrotoxin From the Mediterranean Black Widow Spider (Latrodectus tredecimguttatus)

    doi: 10.3389/fimmu.2020.587825

    Figure Lengend Snippet: Monoclonal IgG ELISA signals against (A) α-LTX and (B) L. tredecimguttatus whole venom. The binding capability of TPL0020_02_G9 to α-LTX was assessed using different concentrations of IgG. The binding specificity was evaluated by testing the binding of the IgG to three controls (binding to milk proteins, streptavidin, and neutravidin) using the highest IgG concentration (2,000 ng/ml). Each column represents the average of triplicate measurements with error bars indicating the standard deviation.

    Article Snippet: ReagentsLyophilized native α-LTX ( > 98% purity) was obtained from Alomone Labs (Jerusalem, Israel, LSP-130).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay, Standard Deviation

    Effect of α-LTX and its mixture with IgG TPL0020_02_G9 at 1:10 ratio (w/w) on spontaneous EPSC frequency in pyramidal neurons from mPFC. (A) Representative recording of α-LTX action. Time course of the experiment and expanded parts in control (1), after 10 min of α-LTX application (2), and after 10 μM DNQX and 100 μM D-APV application (3) are shown. α-LTX causes a strong increase of spontaneous EPSC frequency, and selective antagonists of ionotropic glutamate receptors abolish this effect. (B) Representative recording of α-LTX action in the presence of IgG TPL0020_02_G9. Strong frequency increase is seen only after 20 min of application. (C) Time development of α-LTX effect and its modulation by IgG. Spontaneous EPSC frequencies are normalized to the average control values. The development of effect is strongly delayed in the presence of IgG (red traces) compared to control with α-LTX alone (black traces). (D) Characteristic times when the 3 × SD threshold is reached or spontaneous EPSC frequency is increased four-fold for α-LTX alone (white bars) and in the presence of the IgG (red bars). The differences are significant (p

    Journal: Frontiers in Immunology

    Article Title: Discovery of a Recombinant Human Monoclonal Immunoglobulin G Antibody Against α-Latrotoxin From the Mediterranean Black Widow Spider (Latrodectus tredecimguttatus)

    doi: 10.3389/fimmu.2020.587825

    Figure Lengend Snippet: Effect of α-LTX and its mixture with IgG TPL0020_02_G9 at 1:10 ratio (w/w) on spontaneous EPSC frequency in pyramidal neurons from mPFC. (A) Representative recording of α-LTX action. Time course of the experiment and expanded parts in control (1), after 10 min of α-LTX application (2), and after 10 μM DNQX and 100 μM D-APV application (3) are shown. α-LTX causes a strong increase of spontaneous EPSC frequency, and selective antagonists of ionotropic glutamate receptors abolish this effect. (B) Representative recording of α-LTX action in the presence of IgG TPL0020_02_G9. Strong frequency increase is seen only after 20 min of application. (C) Time development of α-LTX effect and its modulation by IgG. Spontaneous EPSC frequencies are normalized to the average control values. The development of effect is strongly delayed in the presence of IgG (red traces) compared to control with α-LTX alone (black traces). (D) Characteristic times when the 3 × SD threshold is reached or spontaneous EPSC frequency is increased four-fold for α-LTX alone (white bars) and in the presence of the IgG (red bars). The differences are significant (p

    Article Snippet: ReagentsLyophilized native α-LTX ( > 98% purity) was obtained from Alomone Labs (Jerusalem, Israel, LSP-130).

    Techniques:

    Melatonin administration prolongs injury‐induced ERK phosphorylation. A, Phospho‐ERK 1/2 signal ( red ) at LAL NMJs in controls and 24/72 h after α‐LTx injection, w/o melatonin i.p. treatment. PSC are green (GFP‐positive). Scale bars: 5 µm. B, Phospho‐ERK 1/2 signal ( red ) in whole‐mount (left) and cross sections (right) of sciatic nerves before and 3 d after crush (w/o melatonin i.p. treatment). White squares indicate the crush site. PSC are in green . Scale bars: 500 µm (left) and 20 µm (right). C, quantification of p‐ERK signal in cross sections. *** P

    Journal: Journal of Pineal Research

    Article Title: Melatonin promotes regeneration of injured motor axons via MT1 receptors, et al. Melatonin promotes regeneration of injured motor axons via MT1 receptors

    doi: 10.1111/jpi.12695

    Figure Lengend Snippet: Melatonin administration prolongs injury‐induced ERK phosphorylation. A, Phospho‐ERK 1/2 signal ( red ) at LAL NMJs in controls and 24/72 h after α‐LTx injection, w/o melatonin i.p. treatment. PSC are green (GFP‐positive). Scale bars: 5 µm. B, Phospho‐ERK 1/2 signal ( red ) in whole‐mount (left) and cross sections (right) of sciatic nerves before and 3 d after crush (w/o melatonin i.p. treatment). White squares indicate the crush site. PSC are in green . Scale bars: 500 µm (left) and 20 µm (right). C, quantification of p‐ERK signal in cross sections. *** P

    Article Snippet: Purified α‐LTx was obtained by Alomone (cat. LSP‐130).

    Techniques: Injection

    Melatonin promotes nerve terminal regeneration. A, Evoked junctional potentials (EJPs) amplitude of soleus muscles 72 h after α‐LTx injection in the hind limb, w/o melatonin i.p. injections. Each bar represents mean ± SEM from N = 4, number of analyzed fibers: 10, * P

    Journal: Journal of Pineal Research

    Article Title: Melatonin promotes regeneration of injured motor axons via MT1 receptors, et al. Melatonin promotes regeneration of injured motor axons via MT1 receptors

    doi: 10.1111/jpi.12695

    Figure Lengend Snippet: Melatonin promotes nerve terminal regeneration. A, Evoked junctional potentials (EJPs) amplitude of soleus muscles 72 h after α‐LTx injection in the hind limb, w/o melatonin i.p. injections. Each bar represents mean ± SEM from N = 4, number of analyzed fibers: 10, * P

    Article Snippet: Purified α‐LTx was obtained by Alomone (cat. LSP‐130).

    Techniques: Injection

    MT 1 receptors are expressed at the NMJ and along the sciatic nerve and mediate the pro‐regenerative action of melatonin. A, EJPs amplitude of soleus muscles: (a) in control conditions (± luzindole); (b) +α‐LTx ± i.p. daily treatment with melatonin ± luzindole daily local injections (time point: 72 h after injury); (c) +α‐LTx ± luzindole daily local injections (time point: 96 h after injury). Each bar represents mean ± SEM from N = 4 (number of analyzed fibers: 10). * P

    Journal: Journal of Pineal Research

    Article Title: Melatonin promotes regeneration of injured motor axons via MT1 receptors, et al. Melatonin promotes regeneration of injured motor axons via MT1 receptors

    doi: 10.1111/jpi.12695

    Figure Lengend Snippet: MT 1 receptors are expressed at the NMJ and along the sciatic nerve and mediate the pro‐regenerative action of melatonin. A, EJPs amplitude of soleus muscles: (a) in control conditions (± luzindole); (b) +α‐LTx ± i.p. daily treatment with melatonin ± luzindole daily local injections (time point: 72 h after injury); (c) +α‐LTx ± luzindole daily local injections (time point: 96 h after injury). Each bar represents mean ± SEM from N = 4 (number of analyzed fibers: 10). * P

    Article Snippet: Purified α‐LTx was obtained by Alomone (cat. LSP‐130).

    Techniques:

    NUCC-390 promotes functional and anatomical recovery of the NMJ. ( A ) Mice locally injected in the left hind limb with α-LTx were daily treated either with vehicle, or NUCC-390, or AMD3100, or their combinations. Seventy-two hours later, soleus muscles were dissected, and EJPs recorded. * p

    Journal: Cells

    Article Title: An Agonist of the CXCR4 Receptor Strongly Promotes Regeneration of Degenerated Motor Axon Terminals

    doi: 10.3390/cells8101183

    Figure Lengend Snippet: NUCC-390 promotes functional and anatomical recovery of the NMJ. ( A ) Mice locally injected in the left hind limb with α-LTx were daily treated either with vehicle, or NUCC-390, or AMD3100, or their combinations. Seventy-two hours later, soleus muscles were dissected, and EJPs recorded. * p

    Article Snippet: Cytosine β-d -arabinofuranoside hydrochloride (C6645), DNase I from bovine pancreas (DN25), poly-l -lysine hydrobromide (P1274), laminin (L2020) and trypsin (T4799) were from Sigma–Aldrich (Milan, Italy). µ-Conotoxin GIIIB and α-LTx were purchased from Alomone (Jerusalem, Israel).

    Techniques: Functional Assay, Mouse Assay, Injection

    HeLa cells overexpressing mutant ADGRL2 present enhanced cell adhesive properties associated to signal transduction alteration. a-c HeLa cells expressing either pcD-Empty ( a ), CIRL2-Wt ( b ) or CIRL2-Mt ( c ) were labelled with the viability marker, cell tracker green (10 μM), and the mortality marker 7-AAD (50 μg/ml) and incubated at room temperature for 90 min in aggregation medium. Note the marked increase of aggregate sizes in CIRL2-Mt expressing cells. d-f HeLa cells expressing either pcD-Empty ( d ) CIRL2-Wt ( e ) or CIRL2-Mt ( f ) were incubated at room temperature for 90 min in aggregation medium containing the PLC inhibitor U73122 (3 μM). Note that inhibition of PLC enhanced homophilic binding of HeLa cells overexpressing CIRL2-Wt. g-i HeLa cells expressing either pcD-Empty ( g ), CIRL2-Wt ( h ) or CIRL2-Mt ( i ) were incubated at room temperature for 90 min in aggregation medium containing α-latrotoxin (1 nM) which prevented cell aggregation. j-l HeLa cells expressing either pcD-GFP-Empty ( j ), CIRL2-GFP-Wt ( k ) or CRL2-GFP-Mt ( l ) were incubated at room temperature for 90 min in aggregation medium. Cells expressing CIRL2 coupled to GFP in C-terminal were not able to aggregate. m Quantification and statistical analysis of the aggregation index. Each value represents the mean (±S.E.M.) of three independent cell-adhesion assays. **, p

    Journal: Acta Neuropathologica Communications

    Article Title: A de novo variant in ADGRL2 suggests a novel mechanism underlying the previously undescribed association of extreme microcephaly with severely reduced sulcation and rhombencephalosynapsis

    doi: 10.1186/s40478-018-0610-5

    Figure Lengend Snippet: HeLa cells overexpressing mutant ADGRL2 present enhanced cell adhesive properties associated to signal transduction alteration. a-c HeLa cells expressing either pcD-Empty ( a ), CIRL2-Wt ( b ) or CIRL2-Mt ( c ) were labelled with the viability marker, cell tracker green (10 μM), and the mortality marker 7-AAD (50 μg/ml) and incubated at room temperature for 90 min in aggregation medium. Note the marked increase of aggregate sizes in CIRL2-Mt expressing cells. d-f HeLa cells expressing either pcD-Empty ( d ) CIRL2-Wt ( e ) or CIRL2-Mt ( f ) were incubated at room temperature for 90 min in aggregation medium containing the PLC inhibitor U73122 (3 μM). Note that inhibition of PLC enhanced homophilic binding of HeLa cells overexpressing CIRL2-Wt. g-i HeLa cells expressing either pcD-Empty ( g ), CIRL2-Wt ( h ) or CIRL2-Mt ( i ) were incubated at room temperature for 90 min in aggregation medium containing α-latrotoxin (1 nM) which prevented cell aggregation. j-l HeLa cells expressing either pcD-GFP-Empty ( j ), CIRL2-GFP-Wt ( k ) or CRL2-GFP-Mt ( l ) were incubated at room temperature for 90 min in aggregation medium. Cells expressing CIRL2 coupled to GFP in C-terminal were not able to aggregate. m Quantification and statistical analysis of the aggregation index. Each value represents the mean (±S.E.M.) of three independent cell-adhesion assays. **, p

    Article Snippet: Total recording time was 15 min, and the time interval between two acquisitions was 5 s. After 3 min baseline recording, α-latrotoxin (1 nM, Alomone Labs, Jerusalem, Israel) was added in the calcium-free perfusion medium.

    Techniques: Mutagenesis, Transduction, Expressing, Marker, Incubation, Planar Chromatography, Inhibition, Binding Assay

    Signal transduction coupled to G protein is altered in mutant ADGRL2 amniocytes. Intracellular calcium levels were monitored by microfluorimetry using the ratiometric Fura-2 AM calcium probe and results expressed as mean fluorescence intensity (MFI). a α-latrotoxin (1 nM) was applied to wild-type (Wt) and mutant (Mt) cultured amniocytes under extracellular chelated-calcium conditions (EDTA 4 mM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. b α-latrotoxin (1 nM) was applied to Wt amniocytes under chelated-calcium conditions (EDTA 4 mM). Cultured cells were pre-incubated or not with the phospholipase C inhibitor U73122 (10 μM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. c α-latrotoxin (1 nM) was applied to Mt amniocytes under chelated-calcium conditions (EDTA 4 mM). Cultured cells were pre-incubated or not with the phospholipase C inhibitor U73122 (10 μM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. d Quantification and statistical analysis of intracellular calcium levels from the early and late phases in response to α-latrotoxin stimulation. Areas under the curves (AUC) were expressed in arbitrary units (AU). Each value represents the mean (±S.E.M.) of 30 cells. *, p

    Journal: Acta Neuropathologica Communications

    Article Title: A de novo variant in ADGRL2 suggests a novel mechanism underlying the previously undescribed association of extreme microcephaly with severely reduced sulcation and rhombencephalosynapsis

    doi: 10.1186/s40478-018-0610-5

    Figure Lengend Snippet: Signal transduction coupled to G protein is altered in mutant ADGRL2 amniocytes. Intracellular calcium levels were monitored by microfluorimetry using the ratiometric Fura-2 AM calcium probe and results expressed as mean fluorescence intensity (MFI). a α-latrotoxin (1 nM) was applied to wild-type (Wt) and mutant (Mt) cultured amniocytes under extracellular chelated-calcium conditions (EDTA 4 mM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. b α-latrotoxin (1 nM) was applied to Wt amniocytes under chelated-calcium conditions (EDTA 4 mM). Cultured cells were pre-incubated or not with the phospholipase C inhibitor U73122 (10 μM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. c α-latrotoxin (1 nM) was applied to Mt amniocytes under chelated-calcium conditions (EDTA 4 mM). Cultured cells were pre-incubated or not with the phospholipase C inhibitor U73122 (10 μM). Three minutes after α-latrotoxin administration, cells were perfused without EDTA to restore extracellular calcium levels. d Quantification and statistical analysis of intracellular calcium levels from the early and late phases in response to α-latrotoxin stimulation. Areas under the curves (AUC) were expressed in arbitrary units (AU). Each value represents the mean (±S.E.M.) of 30 cells. *, p

    Article Snippet: Total recording time was 15 min, and the time interval between two acquisitions was 5 s. After 3 min baseline recording, α-latrotoxin (1 nM, Alomone Labs, Jerusalem, Israel) was added in the calcium-free perfusion medium.

    Techniques: Transduction, Mutagenesis, Fluorescence, Cell Culture, Incubation