sap102  (Alomone Labs)


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    Alomone Labs sap102
    Sap102, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sap102 - by Bioz Stars, 2022-11
    85/100 stars

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    Alomone Labs rabbit anti sap102
    VE-2B clustered with <t>SAP102</t> at 10 and 45 minutes after release from the ER. (A) At 10-minutes after ER exit VE-2B clearly co-localized with endogenous SAP102 (top panels, VE-2B EGFP fluorescence in green, and endogenous immunostaining with antibody to SAP102 in red; boxes depicts the enlargements; scale bars are 10 µm). At 45 minutes after ER exit (panels second from the top), a time point at which the leading edge of the pulse of VE-2B cargo is arriving at the cell surface (see Fig. 1C), endogenous SAP102 continued to exhibit strong colocalization. VE-2A demonstrated indistinguishable patterns of colocalization with SAP102 along the secretory pathway (summarized in Table S1 ). Colocalization of VE-2B with SAP102 is dependent on the distal C-terminal seven amino acid residues that contain the PDZ-binding domain of NR2B (bottom panels), as VE-2BΔ7 exhibited little colocalization with SAP102. Note that VE-2BΔ7 still exhibited apparent clustering (left panel at bottom; for quantification see Fig. 6E) and that endogenous SAP102 did not concentrate in the perinuclear Golgi region in the absence of bound receptor (bottom red panel). (B) Neurons transfected with VE, or VE-2B were incubated overnight at 40°C, then switched to media incubated at 15°C for 1 hour to block transport to the Golgi apparatus, and limit secretory cargo transport to no further than the IC. Neurons were then immunostained for endogenous SAP102. Concentration of VE was observed along the lengths of dendrites that was consistent with budding and protrusion from ER exits sites and initial transport to the Golgi (top panels; characterized previously [29] ). However, concentrations of VE were not well colocalized with SAP102. Alternatively, concentrations of VE-2B demonstrated the beginnings of co-localization with SAP102 at the IC (bottom panels; scale bars 5 µm). (C) Colocalization was quantified as described in Experimental Methods with 5–15 images of neuronal soma from at least 3 separate transfection experiments for a minimum of 15 and a maximum of 26 measures. To assess whether concentrated clusters of VE-2B were co-localized with concentrated SAP102 clusters, the threshold of SAP102 was held constant at a threshold that included concentrated SAP102 clusters (104-255 gray level, inclusive), and the threshold of inclusion for VE-2B (green threshold) was varied from 52-255 to 182-255 (x-axis). The percent colocalization was averaged within transfection to reduce random error (the number of transfections equals N), and then within-group to obtain the means ± SEM. By one-way Anova with repeated measures, there was a significant group effect (P
    Rabbit Anti Sap102, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti sap102/product/Alomone Labs
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti sap102 - by Bioz Stars, 2022-11
    85/100 stars
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    VE-2B clustered with SAP102 at 10 and 45 minutes after release from the ER. (A) At 10-minutes after ER exit VE-2B clearly co-localized with endogenous SAP102 (top panels, VE-2B EGFP fluorescence in green, and endogenous immunostaining with antibody to SAP102 in red; boxes depicts the enlargements; scale bars are 10 µm). At 45 minutes after ER exit (panels second from the top), a time point at which the leading edge of the pulse of VE-2B cargo is arriving at the cell surface (see Fig. 1C), endogenous SAP102 continued to exhibit strong colocalization. VE-2A demonstrated indistinguishable patterns of colocalization with SAP102 along the secretory pathway (summarized in Table S1 ). Colocalization of VE-2B with SAP102 is dependent on the distal C-terminal seven amino acid residues that contain the PDZ-binding domain of NR2B (bottom panels), as VE-2BΔ7 exhibited little colocalization with SAP102. Note that VE-2BΔ7 still exhibited apparent clustering (left panel at bottom; for quantification see Fig. 6E) and that endogenous SAP102 did not concentrate in the perinuclear Golgi region in the absence of bound receptor (bottom red panel). (B) Neurons transfected with VE, or VE-2B were incubated overnight at 40°C, then switched to media incubated at 15°C for 1 hour to block transport to the Golgi apparatus, and limit secretory cargo transport to no further than the IC. Neurons were then immunostained for endogenous SAP102. Concentration of VE was observed along the lengths of dendrites that was consistent with budding and protrusion from ER exits sites and initial transport to the Golgi (top panels; characterized previously [29] ). However, concentrations of VE were not well colocalized with SAP102. Alternatively, concentrations of VE-2B demonstrated the beginnings of co-localization with SAP102 at the IC (bottom panels; scale bars 5 µm). (C) Colocalization was quantified as described in Experimental Methods with 5–15 images of neuronal soma from at least 3 separate transfection experiments for a minimum of 15 and a maximum of 26 measures. To assess whether concentrated clusters of VE-2B were co-localized with concentrated SAP102 clusters, the threshold of SAP102 was held constant at a threshold that included concentrated SAP102 clusters (104-255 gray level, inclusive), and the threshold of inclusion for VE-2B (green threshold) was varied from 52-255 to 182-255 (x-axis). The percent colocalization was averaged within transfection to reduce random error (the number of transfections equals N), and then within-group to obtain the means ± SEM. By one-way Anova with repeated measures, there was a significant group effect (P

    Journal: PLoS ONE

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    doi: 10.1371/journal.pone.0039585

    Figure Lengend Snippet: VE-2B clustered with SAP102 at 10 and 45 minutes after release from the ER. (A) At 10-minutes after ER exit VE-2B clearly co-localized with endogenous SAP102 (top panels, VE-2B EGFP fluorescence in green, and endogenous immunostaining with antibody to SAP102 in red; boxes depicts the enlargements; scale bars are 10 µm). At 45 minutes after ER exit (panels second from the top), a time point at which the leading edge of the pulse of VE-2B cargo is arriving at the cell surface (see Fig. 1C), endogenous SAP102 continued to exhibit strong colocalization. VE-2A demonstrated indistinguishable patterns of colocalization with SAP102 along the secretory pathway (summarized in Table S1 ). Colocalization of VE-2B with SAP102 is dependent on the distal C-terminal seven amino acid residues that contain the PDZ-binding domain of NR2B (bottom panels), as VE-2BΔ7 exhibited little colocalization with SAP102. Note that VE-2BΔ7 still exhibited apparent clustering (left panel at bottom; for quantification see Fig. 6E) and that endogenous SAP102 did not concentrate in the perinuclear Golgi region in the absence of bound receptor (bottom red panel). (B) Neurons transfected with VE, or VE-2B were incubated overnight at 40°C, then switched to media incubated at 15°C for 1 hour to block transport to the Golgi apparatus, and limit secretory cargo transport to no further than the IC. Neurons were then immunostained for endogenous SAP102. Concentration of VE was observed along the lengths of dendrites that was consistent with budding and protrusion from ER exits sites and initial transport to the Golgi (top panels; characterized previously [29] ). However, concentrations of VE were not well colocalized with SAP102. Alternatively, concentrations of VE-2B demonstrated the beginnings of co-localization with SAP102 at the IC (bottom panels; scale bars 5 µm). (C) Colocalization was quantified as described in Experimental Methods with 5–15 images of neuronal soma from at least 3 separate transfection experiments for a minimum of 15 and a maximum of 26 measures. To assess whether concentrated clusters of VE-2B were co-localized with concentrated SAP102 clusters, the threshold of SAP102 was held constant at a threshold that included concentrated SAP102 clusters (104-255 gray level, inclusive), and the threshold of inclusion for VE-2B (green threshold) was varied from 52-255 to 182-255 (x-axis). The percent colocalization was averaged within transfection to reduce random error (the number of transfections equals N), and then within-group to obtain the means ± SEM. By one-way Anova with repeated measures, there was a significant group effect (P

    Article Snippet: Two separate anti-SAP102, and anti-PSD-95 antibodies have been characterized previously (rabbit anti-SAP102, JH62514; rabbit anti-SAP102, Alomone Labs; rabbit anti-PSD-95, T60; mouse PSD-95, Transduction Labs; .

    Techniques: Fluorescence, Immunostaining, Binding Assay, Transfection, Incubation, Blocking Assay, Concentration Assay

    VE-2B interacted directly with SAP102, and VE-2B, SAP102 and PSD-95 formed co-clusters. (A) Western blotting was performed on cortical neurons infected with VE-2B and immunoprecipitated with i1 antibody to VSVG at 10 minutes and 3 hours after switch to permissive temperature (24 fold enrichment). Immunoblots were performed with rabbit anti-VSVG, PSD-95, and SAP102. Input, unbound, and immunoprecipitation fractions (IP) were run for each blot. To minimize the possibility of false-positives, buffer only was added to the lanes adjacent to the VE-2B IP lanes. Identical film exposure times for both anti-PSD-95 and anti-SAP102 indicate that SAP102 associates at 10 minutes and 3 hours after ER exit whereas PSD-95 does not. Longer film exposure times did not unambiguously indicate that PSD-95 was directly associated. (B) Western blotting was performed on cortical neurons infected with VE and immunoprecipitated with antibody to VSVG at 10 minutes after switch to permissive temperature. Immunoblots were then performed with rabbit anti-VSVG, and SAP102. Input, unbound, and IP fractions were run for each blot. The results indicated that VE (left panel) did not co-immunoprecipitate measurable quantities of SAP102 (right panel). (C) VE-2B transfected neurons 3 hours after ER release were immunostained for PSD-95 (red) and SAP102 (blue; scale bar, 5 µm). Aqua-colored arrows indicate VE-2B co-localized with SAP102 primarily. White arrows indicate VE-2B co-localized with both PSD-95 and SAP102.

    Journal: PLoS ONE

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    doi: 10.1371/journal.pone.0039585

    Figure Lengend Snippet: VE-2B interacted directly with SAP102, and VE-2B, SAP102 and PSD-95 formed co-clusters. (A) Western blotting was performed on cortical neurons infected with VE-2B and immunoprecipitated with i1 antibody to VSVG at 10 minutes and 3 hours after switch to permissive temperature (24 fold enrichment). Immunoblots were performed with rabbit anti-VSVG, PSD-95, and SAP102. Input, unbound, and immunoprecipitation fractions (IP) were run for each blot. To minimize the possibility of false-positives, buffer only was added to the lanes adjacent to the VE-2B IP lanes. Identical film exposure times for both anti-PSD-95 and anti-SAP102 indicate that SAP102 associates at 10 minutes and 3 hours after ER exit whereas PSD-95 does not. Longer film exposure times did not unambiguously indicate that PSD-95 was directly associated. (B) Western blotting was performed on cortical neurons infected with VE and immunoprecipitated with antibody to VSVG at 10 minutes after switch to permissive temperature. Immunoblots were then performed with rabbit anti-VSVG, and SAP102. Input, unbound, and IP fractions were run for each blot. The results indicated that VE (left panel) did not co-immunoprecipitate measurable quantities of SAP102 (right panel). (C) VE-2B transfected neurons 3 hours after ER release were immunostained for PSD-95 (red) and SAP102 (blue; scale bar, 5 µm). Aqua-colored arrows indicate VE-2B co-localized with SAP102 primarily. White arrows indicate VE-2B co-localized with both PSD-95 and SAP102.

    Article Snippet: Two separate anti-SAP102, and anti-PSD-95 antibodies have been characterized previously (rabbit anti-SAP102, JH62514; rabbit anti-SAP102, Alomone Labs; rabbit anti-PSD-95, T60; mouse PSD-95, Transduction Labs; .

    Techniques: Western Blot, Infection, Immunoprecipitation, Transfection

    Relationship between native, full-length NR2s, and VE-NR2 chimeras. (A) Adult rat hippocampal CA1 pyramidal cells were immunostained with antibodies for GM130 (green) and NR2A/B C-termini (red). NR2 clusters co-localized with GM130 (yellow arrows), consistent with native receptor clustering early in the secretory pathway (scale bar 10 µm). (B) Full-length myc-tagged NR2B was transfected for 3.5 hours, and maintained at 20°C for 2.5 additional hours to block progress of myc-NR2B-NR1 beyond the TGN. Cycloheximide (100 µM) was added for the last 1.5 hours to reduce ER staining from recently synthesized myc-NR2B. The results shown above consist of a pulse of myc-NR2B-NR1 heteromeric receptors limited to between the ER and the TGN. Antibody staining for myc (left panel) and SAP102 (middle panel) demonstrated some clustering and co-localization of myc-NR2B with SAP102. Yellow arrows indicate co-localized puncta in the Golgi region, and green arrows indicate diffuse staining consistent with ER (scale bar 10 µm). (C) Immunogold labeling of intracellular NR2A/B (5 nm gold) and SAP102 (10 nm gold) along microtubules in the pyramidal cell body layer of hippocampal CA1 indicated co-localization of NR2A/B and SAP102, which was consistent with NR2A/B and SAP102 association early in the secretory pathway (scale bar is 100 nm). (D) VE-2B was transfected and the following day incubated for 24 hours at 40°C. Full-length myc-NR2B was serially transfected as described in (B) while neurons were incubated at 40°C. After 3 hours at 40°C, neurons were shifted to 20°C incubation for an additional 2.5 hours in the presence of Cycloheximide (100 µM) followed by 30 minutes at 32°C to allow both VE-2B and myc-NR2B to exit the TGN. The top panel shows VE-2B in a proximal dendrite targeted similarly to myc-NR2B (middle panel; scale bar 5 µm) in the same dendrite (bottom panel, merge).

    Journal: PLoS ONE

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    doi: 10.1371/journal.pone.0039585

    Figure Lengend Snippet: Relationship between native, full-length NR2s, and VE-NR2 chimeras. (A) Adult rat hippocampal CA1 pyramidal cells were immunostained with antibodies for GM130 (green) and NR2A/B C-termini (red). NR2 clusters co-localized with GM130 (yellow arrows), consistent with native receptor clustering early in the secretory pathway (scale bar 10 µm). (B) Full-length myc-tagged NR2B was transfected for 3.5 hours, and maintained at 20°C for 2.5 additional hours to block progress of myc-NR2B-NR1 beyond the TGN. Cycloheximide (100 µM) was added for the last 1.5 hours to reduce ER staining from recently synthesized myc-NR2B. The results shown above consist of a pulse of myc-NR2B-NR1 heteromeric receptors limited to between the ER and the TGN. Antibody staining for myc (left panel) and SAP102 (middle panel) demonstrated some clustering and co-localization of myc-NR2B with SAP102. Yellow arrows indicate co-localized puncta in the Golgi region, and green arrows indicate diffuse staining consistent with ER (scale bar 10 µm). (C) Immunogold labeling of intracellular NR2A/B (5 nm gold) and SAP102 (10 nm gold) along microtubules in the pyramidal cell body layer of hippocampal CA1 indicated co-localization of NR2A/B and SAP102, which was consistent with NR2A/B and SAP102 association early in the secretory pathway (scale bar is 100 nm). (D) VE-2B was transfected and the following day incubated for 24 hours at 40°C. Full-length myc-NR2B was serially transfected as described in (B) while neurons were incubated at 40°C. After 3 hours at 40°C, neurons were shifted to 20°C incubation for an additional 2.5 hours in the presence of Cycloheximide (100 µM) followed by 30 minutes at 32°C to allow both VE-2B and myc-NR2B to exit the TGN. The top panel shows VE-2B in a proximal dendrite targeted similarly to myc-NR2B (middle panel; scale bar 5 µm) in the same dendrite (bottom panel, merge).

    Article Snippet: Two separate anti-SAP102, and anti-PSD-95 antibodies have been characterized previously (rabbit anti-SAP102, JH62514; rabbit anti-SAP102, Alomone Labs; rabbit anti-PSD-95, T60; mouse PSD-95, Transduction Labs; .

    Techniques: Transfection, Blocking Assay, Staining, Synthesized, Labeling, Incubation

    Targeting to pre- and postsynaptic markers. (A) Examples of VE-2A, VE-2B, VE-2BΔ7, and VE three hours after exit from the ER immunostained for SAP102 (red), and synaptophysin (Sp; pseudocolored blue), and merged. VE-2B, and VE-2BΔ7 demonstrate significant clustering compared to VE (quantified in E), and targeting to synaptophysin (quantified in D). (B) Higher magnifications of clusters from VE-2B and VE-2BΔ7 seen in A (indicated by boxes) demonstrate roughly equivalent colocalization to SAP102 (quantified in C) and synaptophysin (quantified in D; scale bars 1 µm). (C) VE-2B and VE-2BΔ7 co-localized with postsynaptic SAP102 at 2X background (52–255 inclusive gray scale). By one way Anova (P

    Journal: PLoS ONE

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    doi: 10.1371/journal.pone.0039585

    Figure Lengend Snippet: Targeting to pre- and postsynaptic markers. (A) Examples of VE-2A, VE-2B, VE-2BΔ7, and VE three hours after exit from the ER immunostained for SAP102 (red), and synaptophysin (Sp; pseudocolored blue), and merged. VE-2B, and VE-2BΔ7 demonstrate significant clustering compared to VE (quantified in E), and targeting to synaptophysin (quantified in D). (B) Higher magnifications of clusters from VE-2B and VE-2BΔ7 seen in A (indicated by boxes) demonstrate roughly equivalent colocalization to SAP102 (quantified in C) and synaptophysin (quantified in D; scale bars 1 µm). (C) VE-2B and VE-2BΔ7 co-localized with postsynaptic SAP102 at 2X background (52–255 inclusive gray scale). By one way Anova (P

    Article Snippet: Two separate anti-SAP102, and anti-PSD-95 antibodies have been characterized previously (rabbit anti-SAP102, JH62514; rabbit anti-SAP102, Alomone Labs; rabbit anti-PSD-95, T60; mouse PSD-95, Transduction Labs; .

    Techniques:

    VE-2B and the MAGUKs are consistent with co-transportation to the synapse. (A) VE-2B chimeras co-localized with high intensity PSD-95 (left graph) and SAP102 (right graph) in dendrites 3 hours after release with the red threshold fixed at 4X background (104–255 inclusive gray scale). Colocalization was quantified as described in Experimental Methods. VE, VE-2B, and VE-2BΔ7 colocalization was assessed across the range of inclusive thresholds for green indicated on the x-axis. There was a significant group effect by one-way Anova even at even the lowest green threshold (p

    Journal: PLoS ONE

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    doi: 10.1371/journal.pone.0039585

    Figure Lengend Snippet: VE-2B and the MAGUKs are consistent with co-transportation to the synapse. (A) VE-2B chimeras co-localized with high intensity PSD-95 (left graph) and SAP102 (right graph) in dendrites 3 hours after release with the red threshold fixed at 4X background (104–255 inclusive gray scale). Colocalization was quantified as described in Experimental Methods. VE, VE-2B, and VE-2BΔ7 colocalization was assessed across the range of inclusive thresholds for green indicated on the x-axis. There was a significant group effect by one-way Anova even at even the lowest green threshold (p

    Article Snippet: Two separate anti-SAP102, and anti-PSD-95 antibodies have been characterized previously (rabbit anti-SAP102, JH62514; rabbit anti-SAP102, Alomone Labs; rabbit anti-PSD-95, T60; mouse PSD-95, Transduction Labs; .

    Techniques: