Structured Review

Ipsen Group syntaxin sx
Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), <t>syntaxin</t> (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Syntaxin Sx, supplied by Ipsen Group, 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 sx/product/Ipsen Group
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
syntaxin sx - by Bioz Stars, 2021-03
86/100 stars

Images

1) Product Images from "Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex"

Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2018.08.043

Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Figure Legend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

Techniques Used:

2) Product Images from "Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex"

Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2018.08.043

Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Figure Legend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

Techniques Used:

3) Product Images from "Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly"

Article Title: Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly

Journal: IUCrJ

doi: 10.1107/S2052252514020727

SNARE proteins involved in membrane fusion. ( a ) Domain arrangements of the SNARE proteins: syntaxin, SNAP23/25 and VAMP2 (TMD, transmembrane domain); ( b ) trans -SNARE-complex formation through interaction of SNARE motifs on t-SNARE proteins (syntaxin and SNAP on the target membrane) with the SNARE motif of the v-SNARE protein (VAMP2) on the vesicle membrane; ( c ) cis -SNARE complex with the TMD of syntaxin and VAMP2 on the same membrane. The blue circle labeled ‘N’ is the N-peptide. Palmitoylation anchors for SNAP23/25 are not shown in panels ( b ) and ( c ).
Figure Legend Snippet: SNARE proteins involved in membrane fusion. ( a ) Domain arrangements of the SNARE proteins: syntaxin, SNAP23/25 and VAMP2 (TMD, transmembrane domain); ( b ) trans -SNARE-complex formation through interaction of SNARE motifs on t-SNARE proteins (syntaxin and SNAP on the target membrane) with the SNARE motif of the v-SNARE protein (VAMP2) on the vesicle membrane; ( c ) cis -SNARE complex with the TMD of syntaxin and VAMP2 on the same membrane. The blue circle labeled ‘N’ is the N-peptide. Palmitoylation anchors for SNAP23/25 are not shown in panels ( b ) and ( c ).

Techniques Used: Labeling

4) Product Images from "Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy"

Article Title: Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy

Journal: Croatica chemica acta. Arhiv za kemiju

doi:

Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated
Figure Legend Snippet: Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

Techniques Used:

Related Articles

other:

Article Title: Depolarization-Evoked Secretion Requires Two Vicinal Transmembrane Cysteines of Syntaxin 1A
Article Snippet: The averages of capacitance transients (ΔCm) were: for Sx 1A, 2.65±0.17 nF (n = 18), Sx 2, 1.04±0.13 nF (n = 16), Sx 3, 0.86±0.12 nF (n = 12) and Sx 4, 0.48±0.11 nF, while ΔCm of Cav1.2 alone was 0.7±0.1 nF ( ).

Article Title: Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins
Article Snippet: Although regulation of SNARE complex assembly is not well understood, it is clear that two conserved protein families, the Sx (syntaxin) and the SM (Sec1p/Munc18) proteins, are central to this process.

Injection:

Article Title: Depolarization-Evoked Secretion Requires Two Vicinal Transmembrane Cysteines of Syntaxin 1A
Article Snippet: Oocytes expressing Cav1.2 without, and with Sx 1A, SNAP-25, and SytI (excitosome) were depolarized according to the protocol in , and Cm monitored ( left ). .. Using the same depolarizing protocol, Cm was monitored in oocytes injected with a cRNA mixture of Cav1.2, SytI, SNAP-25 and one of the Sx isoforms, Sx 2, Sx 3 or Sx 4 ( ). ..

Mutagenesis:

Article Title: Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains
Article Snippet: .. Proteins and lipids Syntaxin 1 TMD (residues 266–288; sx-1TM) from Rattus norvegicus , syntaxin 4 TMD (residues 262–297; sx-4TM) from Homo sapiens and syntaxin 1 TMD mutant (sx-1TM with the following mutations: M267A, C271A and I279A) were synthesized using Fmoc solid phase synthesis. .. The fluorescent dyes Atto647N NHS-ester (Atto-Tec) and Rodamine red succinimidyl ester (Life Technologies) were coupled to the N-termini of sx-TM.

Synthesized:

Article Title: Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains
Article Snippet: .. Proteins and lipids Syntaxin 1 TMD (residues 266–288; sx-1TM) from Rattus norvegicus , syntaxin 4 TMD (residues 262–297; sx-4TM) from Homo sapiens and syntaxin 1 TMD mutant (sx-1TM with the following mutations: M267A, C271A and I279A) were synthesized using Fmoc solid phase synthesis. .. The fluorescent dyes Atto647N NHS-ester (Atto-Tec) and Rodamine red succinimidyl ester (Life Technologies) were coupled to the N-termini of sx-TM.

Expressing:

Article Title: Depolarization-Evoked Secretion Requires Two Vicinal Transmembrane Cysteines of Syntaxin 1A
Article Snippet: Discussion We have used a functional reconstituted assay of secretion in Xenopus oocytes as an approach to studying the crosstalk between Sx 1A and VGCC in exocytosis, and a means of examining the role of VGCC activation during the exocytotic events. .. Whole cell membrane capacitance transients were monitored in oocytes expressing the recombinant excitosome complex consisting of Cav1.2, Sx 1A, SNAP-25, and SytI or mixtures where Sx 1A was replaced by Sx1A TMD mutants, the Sx 1A/Sx 2 chimera, truncated Sx 1A, or different Sx isoforms. ..

Recombinant:

Article Title: Depolarization-Evoked Secretion Requires Two Vicinal Transmembrane Cysteines of Syntaxin 1A
Article Snippet: Discussion We have used a functional reconstituted assay of secretion in Xenopus oocytes as an approach to studying the crosstalk between Sx 1A and VGCC in exocytosis, and a means of examining the role of VGCC activation during the exocytotic events. .. Whole cell membrane capacitance transients were monitored in oocytes expressing the recombinant excitosome complex consisting of Cav1.2, Sx 1A, SNAP-25, and SytI or mixtures where Sx 1A was replaced by Sx1A TMD mutants, the Sx 1A/Sx 2 chimera, truncated Sx 1A, or different Sx isoforms. ..

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Ipsen Group syntaxin sx
    Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), <t>syntaxin</t> (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
    Syntaxin Sx, supplied by Ipsen Group, 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 sx/product/Ipsen Group
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    syntaxin sx - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    86
    Ipsen Group target syntaxin sx
    Specificity of <t>Munc18:Syntaxin</t> interactions. Munc18a (cyan) binds Sx1 (magenta) via two tight binding modes (left hand side). One binding mode occurs in the presence of the Sx1 N-peptide, the other in its absence. “Non-cognate” Munc18c (gray) also binds tightly to Sx1, though its interaction with Sx1 lacking the N-peptide is very weak (indicated by dotted line). Munc18c binds more tightly than Munc18a to Sx4 (orange) but neither Munc18 recognises Sx4 lacking its N-peptide. These findings indicate that Munc18a and Munc18c bind Sxs differently. Specifically Munc18a has two tight binding modes/sites for Sx1 one of which does not require the N-peptide binding interaction. Munc18c has one tight binding mode/site for Sx4 or Sx1 that requires the Sx N-peptide.
    Target Syntaxin Sx, supplied by Ipsen Group, 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/target syntaxin sx/product/Ipsen Group
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    target syntaxin sx - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    Image Search Results


    Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

    Journal: Biophysical Journal

    Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

    doi: 10.1016/j.bpj.2018.08.043

    Figure Lengend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

    Article Snippet: Synaptobrevin (Sb) and syntaxin (Sx) both contribute to this complex with one α -helix, whereas SNAP25 consists of two α -helical motifs connected by an unstructured linker loop.

    Techniques:

    Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

    Journal: Croatica chemica acta. Arhiv za kemiju

    Article Title: Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy

    doi:

    Figure Lengend Snippet: Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

    Article Snippet: The core SNARE complex is comprised of synaptobrevin 2 (Sb2), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (Sx) and synaptosome-associated protein of 25 kDa (SNAP25), both located on the plasma membrane.

    Techniques:

    Specificity of Munc18:Syntaxin interactions. Munc18a (cyan) binds Sx1 (magenta) via two tight binding modes (left hand side). One binding mode occurs in the presence of the Sx1 N-peptide, the other in its absence. “Non-cognate” Munc18c (gray) also binds tightly to Sx1, though its interaction with Sx1 lacking the N-peptide is very weak (indicated by dotted line). Munc18c binds more tightly than Munc18a to Sx4 (orange) but neither Munc18 recognises Sx4 lacking its N-peptide. These findings indicate that Munc18a and Munc18c bind Sxs differently. Specifically Munc18a has two tight binding modes/sites for Sx1 one of which does not require the N-peptide binding interaction. Munc18c has one tight binding mode/site for Sx4 or Sx1 that requires the Sx N-peptide.

    Journal: PLoS ONE

    Article Title: Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins

    doi: 10.1371/journal.pone.0187302

    Figure Lengend Snippet: Specificity of Munc18:Syntaxin interactions. Munc18a (cyan) binds Sx1 (magenta) via two tight binding modes (left hand side). One binding mode occurs in the presence of the Sx1 N-peptide, the other in its absence. “Non-cognate” Munc18c (gray) also binds tightly to Sx1, though its interaction with Sx1 lacking the N-peptide is very weak (indicated by dotted line). Munc18c binds more tightly than Munc18a to Sx4 (orange) but neither Munc18 recognises Sx4 lacking its N-peptide. These findings indicate that Munc18a and Munc18c bind Sxs differently. Specifically Munc18a has two tight binding modes/sites for Sx1 one of which does not require the N-peptide binding interaction. Munc18c has one tight binding mode/site for Sx4 or Sx1 that requires the Sx N-peptide.

    Article Snippet: SM proteins are SNARE binding proteins that play a crucial role in the late stages of vesicle docking and fusion, as well as stabilisation of the target Syntaxin (Sx) proteins.

    Techniques: Binding Assay