Review



human e syt1  (OriGene)


Bioz Verified Symbol OriGene is a verified supplier
Bioz Manufacturer Symbol OriGene manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 92
      Buy from Supplier

    Structured Review

    OriGene human e syt1
    Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the <t>E-Syt1</t> construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red
    Human E Syt1, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+e+syt1/Synaptotagmin+1+(SYT1)+Human+qPCR+Template+Standard/pmc06481592-106-13-4
    Average 92 stars, based on 3 article reviews
    human e syt1 - by Bioz Stars, 2026-09
    92/100 stars

    Images

    1) Product Images from "In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins"

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins

    Journal: Methods in molecular biology (Clifton, N.J.)

    doi: 10.1007/978-1-4939-9136-5_15

    Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the E-Syt1 construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red
    Figure Legend Snippet: Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the E-Syt1 construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red

    Techniques Used: Construct, Binding Assay

    E-Syt1 is a Ca2+-dependent lipid transfer protein. (a) On the left: time-course of normalized NBD fluorescence signals of liposomes mixtures in the absence or presence of 100 μM Ca2+ at room temperature. E-Syt1cyto was added at time 0 (protein: lipid ratio 1:1000). On the right: quantification of the increase in NBD fluorescence at the end of the incubation (indicated by an arrow in the left graph). (b) As in (a), but with 1 mM sodium dithionite added three times before addition of E-Syt1cyto. Raw fluorescence values, rather than percent fluorescence changes are shown in this figure. Quantifications of NBD fluorescence before addition of detergent are at right. (c) Bar graphs show the quantification of the percentage of 3H radioactivity in the supernatant (light liposomes) over the sum of the total radioactivity in the supernatant and pellet (light plus heavy liposomes). Mean and SD of three independent experiments
    Figure Legend Snippet: E-Syt1 is a Ca2+-dependent lipid transfer protein. (a) On the left: time-course of normalized NBD fluorescence signals of liposomes mixtures in the absence or presence of 100 μM Ca2+ at room temperature. E-Syt1cyto was added at time 0 (protein: lipid ratio 1:1000). On the right: quantification of the increase in NBD fluorescence at the end of the incubation (indicated by an arrow in the left graph). (b) As in (a), but with 1 mM sodium dithionite added three times before addition of E-Syt1cyto. Raw fluorescence values, rather than percent fluorescence changes are shown in this figure. Quantifications of NBD fluorescence before addition of detergent are at right. (c) Bar graphs show the quantification of the percentage of 3H radioactivity in the supernatant (light liposomes) over the sum of the total radioactivity in the supernatant and pellet (light plus heavy liposomes). Mean and SD of three independent experiments

    Techniques Used: Fluorescence, Incubation, Radioactivity

    Related Articles

    Amplification:

    Article Title: Ca 2+ releases E‐Syt1 autoinhibition to couple ER ‐plasma membrane tethering with lipid transport
    Article Snippet: .. The regions coding for residues 93–1,104 (E‐Syt1 cyto ), 93–941 (SMP‐C2ABCD), 93–634 (SMP‐C2AB), 315–1,104 (C2ABCDE), 624–973 (C2CD), and 936–1,104 (C2E) of human E‐Syt1 were amplified by PCR and cloned using AscI and NotI sites into the pCMV6‐An‐His vector (OriGene) for Expi293 cell expression. .. SMP domain (93–327) of human E‐Syt1 was cloned using NdeI and SalI sites, and PH domain (11–140) of rat PLCδ was cloned using NheI and XhoI sites into pET‐28a vector (Novagen).

    Polymerase Chain Reaction:

    Article Title: Ca 2+ releases E‐Syt1 autoinhibition to couple ER ‐plasma membrane tethering with lipid transport
    Article Snippet: .. The regions coding for residues 93–1,104 (E‐Syt1 cyto ), 93–941 (SMP‐C2ABCD), 93–634 (SMP‐C2AB), 315–1,104 (C2ABCDE), 624–973 (C2CD), and 936–1,104 (C2E) of human E‐Syt1 were amplified by PCR and cloned using AscI and NotI sites into the pCMV6‐An‐His vector (OriGene) for Expi293 cell expression. .. SMP domain (93–327) of human E‐Syt1 was cloned using NdeI and SalI sites, and PH domain (11–140) of rat PLCδ was cloned using NheI and XhoI sites into pET‐28a vector (Novagen).

    Clone Assay:

    Article Title: Ca 2+ releases E‐Syt1 autoinhibition to couple ER ‐plasma membrane tethering with lipid transport
    Article Snippet: .. The regions coding for residues 93–1,104 (E‐Syt1 cyto ), 93–941 (SMP‐C2ABCD), 93–634 (SMP‐C2AB), 315–1,104 (C2ABCDE), 624–973 (C2CD), and 936–1,104 (C2E) of human E‐Syt1 were amplified by PCR and cloned using AscI and NotI sites into the pCMV6‐An‐His vector (OriGene) for Expi293 cell expression. .. SMP domain (93–327) of human E‐Syt1 was cloned using NdeI and SalI sites, and PH domain (11–140) of rat PLCδ was cloned using NheI and XhoI sites into pET‐28a vector (Novagen).

    Article Title: Ring-like oligomers of Synaptotagmins and related C2 domain proteins
    Article Snippet: .. Coding sequences of C2A-E domains from human E-Syt1 was cloned into pCMV6-AN-His vector (OriGene). .. The plasmid was transfected into Expi293 cells (Thermo Fisher Scientific, Grant Island, NY) for protein expression.

    Expressing:

    Article Title: Ca 2+ releases E‐Syt1 autoinhibition to couple ER ‐plasma membrane tethering with lipid transport
    Article Snippet: .. The regions coding for residues 93–1,104 (E‐Syt1 cyto ), 93–941 (SMP‐C2ABCD), 93–634 (SMP‐C2AB), 315–1,104 (C2ABCDE), 624–973 (C2CD), and 936–1,104 (C2E) of human E‐Syt1 were amplified by PCR and cloned using AscI and NotI sites into the pCMV6‐An‐His vector (OriGene) for Expi293 cell expression. .. SMP domain (93–327) of human E‐Syt1 was cloned using NdeI and SalI sites, and PH domain (11–140) of rat PLCδ was cloned using NheI and XhoI sites into pET‐28a vector (Novagen).

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: .. Expression and Purification of E-Syt1 cyto Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).

    Purification:

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: .. Expression and Purification of E-Syt1 cyto Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).

    Plasmid Preparation:

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: .. Expression and Purification of E-Syt1 cyto Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: EcoScint scintillation liquid (National Diagnostics). .. Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).

    Article Title: Ring-like oligomers of Synaptotagmins and related C2 domain proteins
    Article Snippet: .. Coding sequences of C2A-E domains from human E-Syt1 was cloned into pCMV6-AN-His vector (OriGene). .. The plasmid was transfected into Expi293 cells (Thermo Fisher Scientific, Grant Island, NY) for protein expression.

    Construct:

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: .. Expression and Purification of E-Syt1 cyto Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins
    Article Snippet: EcoScint scintillation liquid (National Diagnostics). .. Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct). .. Expi293F cells (ThermoFisher).



    Similar Products

    human e syt1  (OriGene)
    92
    OriGene human e syt1
    Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the <t>E-Syt1</t> construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red
    Human E Syt1, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+e+syt1/Synaptotagmin+1+(SYT1)+Human+qPCR+Template+Standard/pmc06481592-106-13-4
    Average 92 stars, based on 1 article reviews
    human e syt1 - by Bioz Stars, 2026-09
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the E-Syt1 construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins

    doi: 10.1007/978-1-4939-9136-5_15

    Figure Lengend Snippet: Architecture and structure of the E-Syts. (a) Domain organization of the E-Syts and of the E-Syt1 construct used for the membrane tethering and lipid transfer assays. (b) Schematic representation of the putative arrangement of E-Syt1 at ER-PM contacts in the presence of elevated cytosolic Ca2+ (see also [5]). The protein dimerizes via its SMP domain. The C2A and the C2C domains have Ca2+-binding sites. (c) Crystal structure of an E-Syt2 fragment comprising its SMP domain and C2A-C2B domains (PDB code: 4P42). One monomer is shown in full colors and the other in pale colors. The SMP domain is in blue, the C2A domain is in green, and the C2B domain is in yellow. Lipid molecules are represented as sticks in red

    Article Snippet: Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct).

    Techniques: Construct, Binding Assay

    E-Syt1 is a Ca2+-dependent lipid transfer protein. (a) On the left: time-course of normalized NBD fluorescence signals of liposomes mixtures in the absence or presence of 100 μM Ca2+ at room temperature. E-Syt1cyto was added at time 0 (protein: lipid ratio 1:1000). On the right: quantification of the increase in NBD fluorescence at the end of the incubation (indicated by an arrow in the left graph). (b) As in (a), but with 1 mM sodium dithionite added three times before addition of E-Syt1cyto. Raw fluorescence values, rather than percent fluorescence changes are shown in this figure. Quantifications of NBD fluorescence before addition of detergent are at right. (c) Bar graphs show the quantification of the percentage of 3H radioactivity in the supernatant (light liposomes) over the sum of the total radioactivity in the supernatant and pellet (light plus heavy liposomes). Mean and SD of three independent experiments

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: In Vitro Assays to Measure the Membrane Tethering and Lipid Transport Activities of the Extended Synaptotagmins

    doi: 10.1007/978-1-4939-9136-5_15

    Figure Lengend Snippet: E-Syt1 is a Ca2+-dependent lipid transfer protein. (a) On the left: time-course of normalized NBD fluorescence signals of liposomes mixtures in the absence or presence of 100 μM Ca2+ at room temperature. E-Syt1cyto was added at time 0 (protein: lipid ratio 1:1000). On the right: quantification of the increase in NBD fluorescence at the end of the incubation (indicated by an arrow in the left graph). (b) As in (a), but with 1 mM sodium dithionite added three times before addition of E-Syt1cyto. Raw fluorescence values, rather than percent fluorescence changes are shown in this figure. Quantifications of NBD fluorescence before addition of detergent are at right. (c) Bar graphs show the quantification of the percentage of 3H radioactivity in the supernatant (light liposomes) over the sum of the total radioactivity in the supernatant and pellet (light plus heavy liposomes). Mean and SD of three independent experiments

    Article Snippet: Plasmids: pCMV6-AN-His vector (e.g., OriGene) containing the region coding for residues 93–1104 of human E-Syt1 ( see [ 5 , 10 ] for detailed information for making this construct).

    Techniques: Fluorescence, Incubation, Radioactivity