syntaxin 18 Search Results


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Proteintech triton x 100
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Santa Cruz Biotechnology mouse anti stx18
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Proteintech stx18 hpa003019
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
Stx18 Hpa003019, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech munc18c protein
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
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Santa Cruz Biotechnology syntaxin 18
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
Syntaxin 18, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Boster Bio mouse monoclonal anti keratin 18 antibody
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
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Igene Biotechnology Inc syntaxin 18 sirna
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
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Synaptic Systems syntaxin 18
FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, <t>Stx18,</t> and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.
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Image Search Results


FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, Stx18, and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.

Journal: Molecular & Cellular Proteomics

Article Title: Quantitative Proteomics Reveals That Only a Subset of the Endoplasmic Reticulum Contributes to the Phagosome

doi: 10.1074/mcp.m111.016378

Figure Lengend Snippet: FIG. 4. Validation of MS results by confocal microscopy indi- cates that only a subdomain of the ER is recruited to the phago- some. Early PB-IgG phagosomes were formed in J774A.1 cells that were plated on fibronectin-coated cyoverslips. After fixation and per- meabilization, the cells were stained for various proteins detected on the phagosome (e.g. SRP54, Stx18, and SPTLC2) and counterstained with Cnx antibody and phalloidin-BODIPY to reveal nascent phago- somes (“Experimental Procedures”). A, the data indicate that the ER proteins SRP54 and Stx18 co-localize with Cnx on the phagosome, whereas SPTLC2 does not. B, quantification of the relative co-local- ization in whole cells of putative phagosome markers over Cnx using the mean Pearson’s coefficients obtained by the analysis of at least three representative fields for each staining reveal significant differ- ences in the distribution of several ER markers.

Article Snippet: Proteins selected based on the MS data to represent various values in the fold change graph, ER functions, membrane, cytoplasmic, or luminal localization were probed by WB using the following antibodies: lysosome-associated membrane glycoprotein 1 (LAMP1) clone 1D4B (Developmental Studies Hybridoma bank, Iowa City, IA); cytosolic domain of Cnx (gift from Dr. John J. Bergeron), calreticulin (ab14234) (Abcam, Cambridge, UK); BIP/ GRP78 (610978), CD51 (611012), early endosome antigen 1 (EEA1) (610456), / soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) (611898), and signal recognition particle 54 (610940) (BD Biosciences, Franklin Lakes, NJ); signal recognition particle receptor (gift from Dr. Jacques Paiement); D12/USE1, Stx18, and Sec22b (18); Stx4 (hpa001330) and Stx18 (hpa003019) (Sigma-Aldrich); retinol dehydrogenase 11 (LS-C46836), protein-tyrosine phosphatase, nonreceptor type 1 (LS-C7486), and SNAP (LS-C15085) (Lifespan Biosciences, Seattle, WA); Rab1a (11671-1-AP) and SPTLC2 (51012-2-AP) (Proteintech, Chicago, IL); Sar1 (07-692) (Millipore, Billerica, MA); neuropilin (GTX16786) (GeneTex, Irvine, CA); protein dissulfide isomerase (PDI) (SPA-891) (Stressgen, Ann Harbor, MI); and Na/K-ATPase (ma3–928) (Abgent, San Diego, CA).

Techniques: Biomarker Discovery, Confocal Microscopy, Staining

FIG. 5. mVenus-Stx18, but not GFP-KDEL, is localized to the subregion of ER implicated in phagocytosis. A, confocal microscopy of RAW264.7 stable cell line expressing GFP-KDEL in the absence (top panel) or presence (bottom two panels) of interferon- (IFN), which was used to flatten the cell to improve the spatial resolution; GFP and Cnx were detected by immunofluorescence. The bottom panel shows a flattened three-dimensional image rendered from multiple confocal sections obtained through the depth of the cell (the bar represents 10 m). Note the discrepancy in the co-localization of GFP and Cnx, particularly in the perinuclear region and at the cell periphery. B, PB-IgG phagosomes were internalized by RAW264.7 GFP-KDEL and J774A.1 mVenus-Stx18. The cells were stained for Cnx, and F-actin was revealed by phalloidin-BODIPY to identify early phagosomes. C, WB using antibody against Cnx and GFP on phagosomes fraction obtained from the same cell line as described in B were performed to compare the recruitment of Cnx, GFP-KDEL, and mVenus-Stx18 to the phagosome fraction. TCL, total cell lysate; IB, immunoblot; Ph, phagosomes fraction.

Journal: Molecular & Cellular Proteomics

Article Title: Quantitative Proteomics Reveals That Only a Subset of the Endoplasmic Reticulum Contributes to the Phagosome

doi: 10.1074/mcp.m111.016378

Figure Lengend Snippet: FIG. 5. mVenus-Stx18, but not GFP-KDEL, is localized to the subregion of ER implicated in phagocytosis. A, confocal microscopy of RAW264.7 stable cell line expressing GFP-KDEL in the absence (top panel) or presence (bottom two panels) of interferon- (IFN), which was used to flatten the cell to improve the spatial resolution; GFP and Cnx were detected by immunofluorescence. The bottom panel shows a flattened three-dimensional image rendered from multiple confocal sections obtained through the depth of the cell (the bar represents 10 m). Note the discrepancy in the co-localization of GFP and Cnx, particularly in the perinuclear region and at the cell periphery. B, PB-IgG phagosomes were internalized by RAW264.7 GFP-KDEL and J774A.1 mVenus-Stx18. The cells were stained for Cnx, and F-actin was revealed by phalloidin-BODIPY to identify early phagosomes. C, WB using antibody against Cnx and GFP on phagosomes fraction obtained from the same cell line as described in B were performed to compare the recruitment of Cnx, GFP-KDEL, and mVenus-Stx18 to the phagosome fraction. TCL, total cell lysate; IB, immunoblot; Ph, phagosomes fraction.

Article Snippet: Proteins selected based on the MS data to represent various values in the fold change graph, ER functions, membrane, cytoplasmic, or luminal localization were probed by WB using the following antibodies: lysosome-associated membrane glycoprotein 1 (LAMP1) clone 1D4B (Developmental Studies Hybridoma bank, Iowa City, IA); cytosolic domain of Cnx (gift from Dr. John J. Bergeron), calreticulin (ab14234) (Abcam, Cambridge, UK); BIP/ GRP78 (610978), CD51 (611012), early endosome antigen 1 (EEA1) (610456), / soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) (611898), and signal recognition particle 54 (610940) (BD Biosciences, Franklin Lakes, NJ); signal recognition particle receptor (gift from Dr. Jacques Paiement); D12/USE1, Stx18, and Sec22b (18); Stx4 (hpa001330) and Stx18 (hpa003019) (Sigma-Aldrich); retinol dehydrogenase 11 (LS-C46836), protein-tyrosine phosphatase, nonreceptor type 1 (LS-C7486), and SNAP (LS-C15085) (Lifespan Biosciences, Seattle, WA); Rab1a (11671-1-AP) and SPTLC2 (51012-2-AP) (Proteintech, Chicago, IL); Sar1 (07-692) (Millipore, Billerica, MA); neuropilin (GTX16786) (GeneTex, Irvine, CA); protein dissulfide isomerase (PDI) (SPA-891) (Stressgen, Ann Harbor, MI); and Na/K-ATPase (ma3–928) (Abgent, San Diego, CA).

Techniques: Confocal Microscopy, Stable Transfection, Expressing, Immunofluorescence, Staining, Western Blot