mouse monoclonal anti syntaxin 1a  (Synaptic Systems)


Bioz Manufacturer Symbol Synaptic Systems manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Synaptic Systems mouse monoclonal anti syntaxin 1a
    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and <t>syntaxin-1</t> helices into the jxt linkers, which leads to fast membrane fusion.
    Mouse Monoclonal Anti Syntaxin 1a, supplied by Synaptic Systems, 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/mouse monoclonal anti syntaxin 1a/product/Synaptic Systems
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal anti syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface"

    Article Title: Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface

    Journal: bioRxiv

    doi: 10.1101/2024.06.17.599435

    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and syntaxin-1 helices into the jxt linkers, which leads to fast membrane fusion.
    Figure Legend Snippet: (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and syntaxin-1 helices into the jxt linkers, which leads to fast membrane fusion.

    Techniques Used: Labeling, Membrane, Binding Assay


    Structured Review

    Millipore anti syntaxin 1a mouse antibody
    Anti Syntaxin 1a Mouse Antibody, supplied by Millipore, 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/anti syntaxin 1a mouse antibody/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti syntaxin 1a mouse antibody - by Bioz Stars, 2024-07
    86/100 stars

    Images


    Structured Review

    GenScript corporation mouse syntaxin 1a
    Mouse Syntaxin 1a, supplied by GenScript corporation, 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/mouse syntaxin 1a/product/GenScript corporation
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images


    Structured Review

    Santa Cruz Biotechnology syntaxin 1a
    KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of <t>STX1A</t> ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, <t>syntaxin</t> <t>1A.</t>
    Syntaxin 1a, supplied by Santa Cruz Biotechnology, 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/syntaxin 1a/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "KSRP improves pancreatic beta cell function and survival"

    Article Title: KSRP improves pancreatic beta cell function and survival

    Journal: Scientific Reports

    doi: 10.1038/s41598-024-55505-8

    KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of STX1A ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, syntaxin 1A.
    Figure Legend Snippet: KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of STX1A ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, syntaxin 1A.

    Techniques Used: Expressing, Western Blot, Binding Assay

    Effects of KSRP knockdown on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 70 nmol/l of siRNA using Lipofectamine RNAiMAX in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA expression of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t-test. (n = 3–7). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α.
    Figure Legend Snippet: Effects of KSRP knockdown on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 70 nmol/l of siRNA using Lipofectamine RNAiMAX in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA expression of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t-test. (n = 3–7). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α.

    Techniques Used: Cell Function Assay, Western Blot, Transfection, Concentration Assay, Staining, Expressing, Binding Assay

    Effects of KSRP overexpression on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 500 ng of plasmid pEGFP-C1 (control) or pEGFP-C1-KSRP in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA analysis of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t test (n = 3–6). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original blots/gels are presented in Supplementary Figs. , . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α .
    Figure Legend Snippet: Effects of KSRP overexpression on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 500 ng of plasmid pEGFP-C1 (control) or pEGFP-C1-KSRP in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA analysis of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t test (n = 3–6). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original blots/gels are presented in Supplementary Figs. , . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α .

    Techniques Used: Over Expression, Cell Function Assay, Western Blot, Transfection, Plasmid Preparation, Concentration Assay, Staining, Binding Assay

    syntaxin 1a liposomes  (Danaher Inc)


    Bioz Verified Symbol Danaher Inc is a verified supplier
    Bioz Manufacturer Symbol Danaher Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Danaher Inc syntaxin 1a liposomes
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a Liposomes, supplied by Danaher Inc, 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/syntaxin 1a liposomes/product/Danaher Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a liposomes - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions"

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    Journal: eLife

    doi: 10.7554/eLife.88619

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Figure Legend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Techniques Used: In Vitro, Mutagenesis, Two Tailed Test


    Figure Legend Snippet:

    Techniques Used: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    syntaxin 1a  (Qiagen)


    Bioz Manufacturer Symbol Qiagen manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Qiagen syntaxin 1a
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a, supplied by Qiagen, 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/syntaxin 1a/product/Qiagen
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions"

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    Journal: eLife

    doi: 10.7554/eLife.88619

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Figure Legend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Techniques Used: In Vitro, Mutagenesis, Two Tailed Test


    Figure Legend Snippet:

    Techniques Used: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    syntaxin 1a  (Agilent technologies)


    Bioz Verified Symbol Agilent technologies is a verified supplier
    Bioz Manufacturer Symbol Agilent technologies manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Agilent technologies syntaxin 1a
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles <t>(GUVs)</t> in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a, supplied by Agilent technologies, 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/syntaxin 1a/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions"

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    Journal: eLife

    doi: 10.7554/eLife.88619

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Figure Legend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Techniques Used: In Vitro, Mutagenesis, Two Tailed Test


    Figure Legend Snippet:

    Techniques Used: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    syntaxin 1a  (Thermo Fisher)


    Bioz Verified Symbol Thermo Fisher is a verified supplier
    Bioz Manufacturer Symbol Thermo Fisher manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Thermo Fisher syntaxin 1a
    Syntaxin 1a, supplied by Thermo Fisher, 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/syntaxin 1a/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images


    Structured Review

    Exosome Diagnostics syntaxin 1a
    Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category
    Syntaxin 1a, supplied by Exosome Diagnostics, 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/syntaxin 1a/product/Exosome Diagnostics
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "The impact of environmental contaminants on extracellular vesicles and their key molecular regulators: A literature and database-driven review"

    Article Title: The impact of environmental contaminants on extracellular vesicles and their key molecular regulators: A literature and database-driven review

    Journal: Environmental and molecular mutagenesis

    doi: 10.1002/em.22522

    Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category
    Figure Legend Snippet: Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category

    Techniques Used: Membrane, Binding Assay, Zinc-Fingers

    reconstitution experiments syntaxin 1a  (New England Biolabs)


    Bioz Verified Symbol New England Biolabs is a verified supplier
    Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    New England Biolabs reconstitution experiments syntaxin 1a
    Reconstitution Experiments Syntaxin 1a, supplied by New England Biolabs, 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/reconstitution experiments syntaxin 1a/product/New England Biolabs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    reconstitution experiments syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars

    Images

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Synaptic Systems mouse monoclonal anti syntaxin 1a
    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and <t>syntaxin-1</t> helices into the jxt linkers, which leads to fast membrane fusion.
    Mouse Monoclonal Anti Syntaxin 1a, supplied by Synaptic Systems, 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/mouse monoclonal anti syntaxin 1a/product/Synaptic Systems
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal anti syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Millipore anti syntaxin 1a mouse antibody
    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and <t>syntaxin-1</t> helices into the jxt linkers, which leads to fast membrane fusion.
    Anti Syntaxin 1a Mouse Antibody, supplied by Millipore, 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/anti syntaxin 1a mouse antibody/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti syntaxin 1a mouse antibody - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    GenScript corporation mouse syntaxin 1a
    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and <t>syntaxin-1</t> helices into the jxt linkers, which leads to fast membrane fusion.
    Mouse Syntaxin 1a, supplied by GenScript corporation, 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/mouse syntaxin 1a/product/GenScript corporation
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Santa Cruz Biotechnology syntaxin 1a
    KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of <t>STX1A</t> ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, <t>syntaxin</t> <t>1A.</t>
    Syntaxin 1a, supplied by Santa Cruz Biotechnology, 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/syntaxin 1a/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Danaher Inc syntaxin 1a liposomes
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a Liposomes, supplied by Danaher Inc, 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/syntaxin 1a liposomes/product/Danaher Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a liposomes - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Qiagen syntaxin 1a
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a, supplied by Qiagen, 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/syntaxin 1a/product/Qiagen
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Agilent technologies syntaxin 1a
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles <t>(GUVs)</t> in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a, supplied by Agilent technologies, 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/syntaxin 1a/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Thermo Fisher syntaxin 1a
    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with <t>syntaxin-1A</t> giant unilamellar vesicles <t>(GUVs)</t> in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.
    Syntaxin 1a, supplied by Thermo Fisher, 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/syntaxin 1a/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    Exosome Diagnostics syntaxin 1a
    Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category
    Syntaxin 1a, supplied by Exosome Diagnostics, 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/syntaxin 1a/product/Exosome Diagnostics
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    86
    New England Biolabs reconstitution experiments syntaxin 1a
    Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category
    Reconstitution Experiments Syntaxin 1a, supplied by New England Biolabs, 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/reconstitution experiments syntaxin 1a/product/New England Biolabs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    reconstitution experiments syntaxin 1a - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    Image Search Results


    (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and syntaxin-1 helices into the jxt linkers, which leads to fast membrane fusion.

    Journal: bioRxiv

    Article Title: Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface

    doi: 10.1101/2024.06.17.599435

    Figure Lengend Snippet: (A) Map of residues that (B) modulate priming function. (C) Map of residues that (D) modulate spontaneous fusion clamping function. (E) Map of residues that modulate (F) Ca 2+ -triggered release probability. In A, C and E, molecular graphics of the C2B domain-SNARE complex interaction from PDB accession code 5CCH . Proteins are represented by ribbon diagrams and sphere models. Carbons are represented in salmon color (SNARE complex) or green (Syt1 C2B domain). Selected residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. In B, D and F, residues are labeled in red if they show a significantly increased response compared to WT rescue, grey if they are not significantly different from WT rescue and blue if they are significantly decreased compared to their respective WT rescue protein. The black dotted line represents WT rescue whereas the dark blue dotted line symbolizes the result for Syt1/Syt7 DKO response. (G) Model of how Syt1 triggers neurotransmitter release. In the primed, fusion clamped state of the release apparatus, the Syt1 C 2 B domain (orange) binds to the SNARE complex through the primary interface and to the plasma membrane through a polybasic region. Regions I and II are represented schematically with pink diamond shape forms. Binding of Ca 2+ (blue circles) induces reorientation of the C 2 B domain to allow insertion of both Ca 2+ binding loops into the plasma membrane and coordination of the Ca 2+ ions by the C 2 B domain ligands and phospholipid head groups. Because of the reorientation, region I dissociates, but region II remains in contact, which in turn communicates a “rowing force” from the Syt C2B reorientation onto the SNARE complex that facilitates extension of the synaptobrevin and syntaxin-1 helices into the jxt linkers, which leads to fast membrane fusion.

    Article Snippet: After blocking with 5 % milk powder (Carl Roth GmbH) for 1 hour at room temperature, membranes were incubated with mouse monoclonal anti-syntaxin-1A (1:10,000; Synaptic Systems), mouse anti-Syt1 (1:1,000; Synaptic Systems), mouse anti-SNAP25 (1:10,000; Synaptic Systems) and mouse monoclonal anti-betaTubulinIII (1:10,000; Sigma) antibodies for 1 hour at room temperature.

    Techniques: Labeling, Membrane, Binding Assay

    KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of STX1A ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, syntaxin 1A.

    Journal: Scientific Reports

    Article Title: KSRP improves pancreatic beta cell function and survival

    doi: 10.1038/s41598-024-55505-8

    Figure Lengend Snippet: KSRP expression decreases in INS-1E cells exposed to palmitate. mRNA analysis of INS2 ( a ), BiP ( b ), CHOP ( c ), and KSRP ( d ) normalized by HPRT after 24 h treatment with 0.5 mmol/l of palmitate. The results were expressed as media ± SEM and were submitted to Student’s t test (n = 3–5). Western blot analysis of STX1A ( e ), BiP ( f ), and KSRP ( g ) proteins normalized by GAPDH after exposure to 0.5 mmol/l of palmitate (12 h, 16 h, or 24 h) in INS-1E cells. The results were expressed as media ± SEM and were submitted to Kruskal–Wallis followed by Dunn’s test ( e ), or One-way ANOVA ( f and g ) (n = 5–6). *p ≤ 0.05. All experiments were performed in simplicate. The membranes were cut prior to the exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, syntaxin 1A.

    Article Snippet: Membranes were incubated with specific primary antibodies: KSRP (HPA034739, Sigma), phospho-eukaryotic translation initiation factor 2α (p-eIF2α, ab32157, Abcam), C/EBP homologous protein (CHOP, ab11419, Abcam), syntaxin 1A (STX1A, sc-12736, Santa Cruz Biotechnology), immunoglobulin binding protein (GRP78/BiP, ab21685, Abcam), inositol-requiring enzyme type 1 (IRE1, ab37073, Abcam), and the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH, G9545, Sigma).

    Techniques: Expressing, Western Blot, Binding Assay

    Effects of KSRP knockdown on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 70 nmol/l of siRNA using Lipofectamine RNAiMAX in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA expression of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t-test. (n = 3–7). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α.

    Journal: Scientific Reports

    Article Title: KSRP improves pancreatic beta cell function and survival

    doi: 10.1038/s41598-024-55505-8

    Figure Lengend Snippet: Effects of KSRP knockdown on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 70 nmol/l of siRNA using Lipofectamine RNAiMAX in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA expression of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t-test. (n = 3–7). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original images for blots are presented in Supplementary Figs. – . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α.

    Article Snippet: Membranes were incubated with specific primary antibodies: KSRP (HPA034739, Sigma), phospho-eukaryotic translation initiation factor 2α (p-eIF2α, ab32157, Abcam), C/EBP homologous protein (CHOP, ab11419, Abcam), syntaxin 1A (STX1A, sc-12736, Santa Cruz Biotechnology), immunoglobulin binding protein (GRP78/BiP, ab21685, Abcam), inositol-requiring enzyme type 1 (IRE1, ab37073, Abcam), and the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH, G9545, Sigma).

    Techniques: Cell Function Assay, Western Blot, Transfection, Concentration Assay, Staining, Expressing, Binding Assay

    Effects of KSRP overexpression on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 500 ng of plasmid pEGFP-C1 (control) or pEGFP-C1-KSRP in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA analysis of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t test (n = 3–6). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original blots/gels are presented in Supplementary Figs. , . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α .

    Journal: Scientific Reports

    Article Title: KSRP improves pancreatic beta cell function and survival

    doi: 10.1038/s41598-024-55505-8

    Figure Lengend Snippet: Effects of KSRP overexpression on beta cell function and survival. mRNA analysis of KSRP normalized by HPRT ( a ) and western blot analysis of KSRP normalized by GAPDH ( b ), 48 h after transfection with 500 ng of plasmid pEGFP-C1 (control) or pEGFP-C1-KSRP in INS-1E cells. Insulin secretion from INS-1E cells exposed to low (2.8 mM) and high (22.2 mM) glucose concentration ( c ). Representative images and percentage of dead cells ( d ) co-stained with Hoechst 33342 (blue) and propidium iodide (red), pictured and determined by the High Content Image System in ImageXpress Micro Confocal. mRNA analysis of INS2 ( e ), BiP ( f ), ATF4 ( g ), and CHOP ( h ) normalized by HPRT in INS-1E transfected cells. Western blot analysis of STX1A ( i ), BiP ( j ), IRE ( k ), and p-eIF2α ( l ) normalized by GAPDH in INS-1E transfected cells. The results were expressed as media ± SEM and submitted to Student’s t test (n = 3–6). *p ≤ 0.05. Insulin secretion and cell death experiments were performed in triplicates and the other experiments in simplicate. The membranes were cut prior to exposure so that only the portion of gel containing the desired bands would be visualized. Original blots/gels are presented in Supplementary Figs. , . ATF4, activating transcription factor 4; BiP, binding immunoglobulin protein; CHOP, C/EBP homologous protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; INS2, insulin 2; IRE1, inositol-requiring enzyme 1; HPRT, hypoxanthine phosphoribosyltransferase; KSRP, KH-type splicing regulatory protein; STX1A, Syntaxin 1A; p-eIF2α, eukaryotic translation initiation factor 2α .

    Article Snippet: Membranes were incubated with specific primary antibodies: KSRP (HPA034739, Sigma), phospho-eukaryotic translation initiation factor 2α (p-eIF2α, ab32157, Abcam), C/EBP homologous protein (CHOP, ab11419, Abcam), syntaxin 1A (STX1A, sc-12736, Santa Cruz Biotechnology), immunoglobulin binding protein (GRP78/BiP, ab21685, Abcam), inositol-requiring enzyme type 1 (IRE1, ab37073, Abcam), and the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH, G9545, Sigma).

    Techniques: Over Expression, Cell Function Assay, Western Blot, Transfection, Plasmid Preparation, Concentration Assay, Staining, Binding Assay

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Article Snippet: Briefly, t-SNARE or syntaxin-1A liposomes (1.25 µmol lipid) were loaded onto a midi column (GE Healthcare) equilibrated with desalting buffer 2 containing trehalose (1 mM HEPES–KOH, pH 7.5, 0.5 wt/vol% glycerol, 10 µM EGTA–KOH, pH 7.4, 50 µM MgCl 2 , 1 mM DTT, 10 mM trehalose).

    Techniques: In Vitro, Mutagenesis, Two Tailed Test

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet:

    Article Snippet: Briefly, t-SNARE or syntaxin-1A liposomes (1.25 µmol lipid) were loaded onto a midi column (GE Healthcare) equilibrated with desalting buffer 2 containing trehalose (1 mM HEPES–KOH, pH 7.5, 0.5 wt/vol% glycerol, 10 µM EGTA–KOH, pH 7.4, 50 µM MgCl 2 , 1 mM DTT, 10 mM trehalose).

    Techniques: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Article Snippet: Syntaxin-1A was eluted from Ni-NTA beads (QIAGEN) by overnight cleavage with Prescission protease (GE Healthcare) at 4°C, removing the His6 tag.

    Techniques: In Vitro, Mutagenesis, Two Tailed Test

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet:

    Article Snippet: Syntaxin-1A was eluted from Ni-NTA beads (QIAGEN) by overnight cleavage with Prescission protease (GE Healthcare) at 4°C, removing the His6 tag.

    Techniques: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet: ( A–C ) In vitro lipid mixing assays of VAMP/Syt1 small unilamellar vesicles (SUVs) with syntaxin-1A giant unilamellar vesicles (GUVs) in the presence of soluble SNAP25b. V48F and D166Y mutants showed impaired fusion clamping in the absence (left) or presence (right) of complexin-II; I67N (red) showed impaired Ca 2+ -independent and Ca 2+ -triggered fusion. Bar diagrams show lipid mixing just before (pre) and after (post) Ca 2+ addition and at the end of the reaction. Mean ± standard error of the mean (SEM; n = 3). ****p < 0.0001; ***p < 0.001; **p < 0.01; *p < 0.05, analysis of variance (ANOVA) with Dunnett’s multiple comparisons test, comparing each mutation to the corresponding wildtype (WT) condition. ( D ) SNAP25b D166Y showed enhanced interactions with SUVs carrying reconstituted syntaxin-1A (Stx-1), VAMP2, Syt1/VAMP2, or an SUV mixture containing Syntaxin-1A and VAMP2/Syt1 in co-flotation assays, whereas V48F displayed weaker increases in interactions with SUVs containing syntaxin-1A, or Syt1/VAMP2. Shown is mean ± SEM on a logarithmic scale. ***p < 0.001, **p < 0.01, *p < 0.05, two-tailed one-sample t -test comparing to 1. Figure 9—source data 1. Excel file containing quantitative data.

    Article Snippet: After 10 min on ice, 100 µl of the GUV–SUV mixes were transferred into a prewarmed 96-well plate (37°C) and fluorescence emitted by Atto488 ( λ ex = 485 nm, λ em = 538 nm) was measured in a Synergy 4 plate reader (BioTek Instruments GmbH) at intervals of 10 s. Ca 2+ was added to a final free concentration of 100 µM ( https://somapp.ucdmc.ucdavis.edu/pharmacology/bers/maxchelator/CaEGTA-TS.htm ) after 2 or 30 min for t-SNARE-GUVs or syntaxin-1A-GUVs, respectively.

    Techniques: In Vitro, Mutagenesis, Two Tailed Test

    Journal: eLife

    Article Title: SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions

    doi: 10.7554/eLife.88619

    Figure Lengend Snippet:

    Article Snippet: After 10 min on ice, 100 µl of the GUV–SUV mixes were transferred into a prewarmed 96-well plate (37°C) and fluorescence emitted by Atto488 ( λ ex = 485 nm, λ em = 538 nm) was measured in a Synergy 4 plate reader (BioTek Instruments GmbH) at intervals of 10 s. Ca 2+ was added to a final free concentration of 100 µM ( https://somapp.ucdmc.ucdavis.edu/pharmacology/bers/maxchelator/CaEGTA-TS.htm ) after 2 or 30 min for t-SNARE-GUVs or syntaxin-1A-GUVs, respectively.

    Techniques: Transfection, Construct, Recombinant, In Vitro, Expressing, Sequencing, Bicinchoninic Acid Protein Assay, Mutagenesis, Western Blot, Buffer Exchange, Software

    Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category

    Journal: Environmental and molecular mutagenesis

    Article Title: The impact of environmental contaminants on extracellular vesicles and their key molecular regulators: A literature and database-driven review

    doi: 10.1002/em.22522

    Figure Lengend Snippet: Genes associated with regulation of EV production, packaging, and release summarized by gene name, function, and EV category

    Article Snippet: STX1A , Syntaxin 1A , Release , Exosome , 1.

    Techniques: Membrane, Binding Assay, Zinc-Fingers