rrid host species type tgn46 bio rad Search Results


ahp500g rrid ab 323104  (Bio-Rad)
96
Bio-Rad ahp500g rrid ab 323104
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Ahp500g Rrid Ab 323104, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rrid+host+species+type+tgn46+bio+rad/pmc07315779-5-9-5?v=Bio-Rad
Average 96 stars, based on 1 article reviews
ahp500g rrid ab 323104 - by Bioz Stars, 2026-08
96/100 stars
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anti trans golgi network protein 2  (Proteintech)
94
Proteintech anti trans golgi network protein 2
KEY RESOURCES TABLE
Anti Trans Golgi Network Protein 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rrid+host+species+type+tgn46+bio+rad/pmc09864477-240-25-32?v=Proteintech
Average 94 stars, based on 1 article reviews
anti trans golgi network protein 2 - by Bioz Stars, 2026-08
94/100 stars
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kda tgn46 antibody antibody  (Novus Biologicals)
93
Novus Biologicals kda tgn46 antibody antibody
Figure 4. The knockdown of CRT downregulated the cell surface expression of E-cadherin in BeWo cells. (a) After 48-h treatment with forskolin (80 mM), the intracellular localization of E-cadherin (green) and CNX (red) was examined in WT, control-shRNA, and CRT-shRNA2 cells using immunofluorescence microscopy with specific antibodies, as described in “Materials and Methods.” CNX was stained as a location marker of the ER. Original magnification, 3400. (b) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and GM130 (red) was examined using specific antibodies, as described in (a). GM130 was stained as a location marker of the cis-Golgi. (c) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and <t>TGN46</t> (red) was examined using specific antibodies, as described in (a). TGN46 was stained as a location marker of the trans-Golgi. (d) The cell surface expression of E-cadherin was examined in the control-shRNA and CRT-shRNA2 cells using the protein biotinylation and avidin pull-down assays, as described in “Materials and Methods.” Data are shown as the mean 6 SD of three independent experiments. *P , 0.05 vs control-shRNA. (e) The subcellular fractionation of the control-shRNA and CRT- shRNA2 cell lysates was conducted via discontinuous sucrose density-gradient centrifugation. The cell lysates were separated into 12 fractions (F), as described in “Materials and Methods.” The expression levels of E-cadherin, Na+/K+ ATPase (cell surface), TGN46 (trans-Golgi), GM130 (cis- Golgi), CNX, CRT, and BiP (ER) were examined in the control-shRNA and CRT-shRNA2 cells, using immunoblot analysis and specific antibodies (fractions 2 to 3; trans-Golgi; fractions 4 to 6, plasma membrane; fractions 8 to 10, cis-Golgi; fractions 9 to 12, ER).
Kda Tgn46 Antibody Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rrid+host+species+type+tgn46+bio+rad/pm30551188-31-129-132?v=Novus+Biologicals
Average 93 stars, based on 1 article reviews
kda tgn46 antibody antibody - by Bioz Stars, 2026-08
93/100 stars
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Image Search Results


KEY RESOURCES TABLE

Journal: Cell reports

Article Title: The Parkinson’s Disease Protein LRRK2 Interacts with the GARP Complex to Promote Retrograde Transport to the trans -Golgi Network

doi: 10.1016/j.celrep.2020.107614

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: sheep anti-TGN46 (human specific) , Biorad , cat # AHP500G; RRID:AB_323104.

Techniques: Clone Assay, Recombinant, Generated, Expressing, Knock-Out, Real-time Polymerase Chain Reaction, Western Blot, RNAscope, Plasmid Preparation, Software

Figure 4. The knockdown of CRT downregulated the cell surface expression of E-cadherin in BeWo cells. (a) After 48-h treatment with forskolin (80 mM), the intracellular localization of E-cadherin (green) and CNX (red) was examined in WT, control-shRNA, and CRT-shRNA2 cells using immunofluorescence microscopy with specific antibodies, as described in “Materials and Methods.” CNX was stained as a location marker of the ER. Original magnification, 3400. (b) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and GM130 (red) was examined using specific antibodies, as described in (a). GM130 was stained as a location marker of the cis-Golgi. (c) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and TGN46 (red) was examined using specific antibodies, as described in (a). TGN46 was stained as a location marker of the trans-Golgi. (d) The cell surface expression of E-cadherin was examined in the control-shRNA and CRT-shRNA2 cells using the protein biotinylation and avidin pull-down assays, as described in “Materials and Methods.” Data are shown as the mean 6 SD of three independent experiments. *P , 0.05 vs control-shRNA. (e) The subcellular fractionation of the control-shRNA and CRT- shRNA2 cell lysates was conducted via discontinuous sucrose density-gradient centrifugation. The cell lysates were separated into 12 fractions (F), as described in “Materials and Methods.” The expression levels of E-cadherin, Na+/K+ ATPase (cell surface), TGN46 (trans-Golgi), GM130 (cis- Golgi), CNX, CRT, and BiP (ER) were examined in the control-shRNA and CRT-shRNA2 cells, using immunoblot analysis and specific antibodies (fractions 2 to 3; trans-Golgi; fractions 4 to 6, plasma membrane; fractions 8 to 10, cis-Golgi; fractions 9 to 12, ER).

Journal: Endocrinology

Article Title: Calreticulin Regulates Syncytialization Through Control of the Synthesis and Transportation of E-Cadherin in BeWo Cells.

doi: 10.1210/en.2018-00868

Figure Lengend Snippet: Figure 4. The knockdown of CRT downregulated the cell surface expression of E-cadherin in BeWo cells. (a) After 48-h treatment with forskolin (80 mM), the intracellular localization of E-cadherin (green) and CNX (red) was examined in WT, control-shRNA, and CRT-shRNA2 cells using immunofluorescence microscopy with specific antibodies, as described in “Materials and Methods.” CNX was stained as a location marker of the ER. Original magnification, 3400. (b) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and GM130 (red) was examined using specific antibodies, as described in (a). GM130 was stained as a location marker of the cis-Golgi. (c) After 48-h treatment with forskolin, the intracellular localization of E-cadherin (green) and TGN46 (red) was examined using specific antibodies, as described in (a). TGN46 was stained as a location marker of the trans-Golgi. (d) The cell surface expression of E-cadherin was examined in the control-shRNA and CRT-shRNA2 cells using the protein biotinylation and avidin pull-down assays, as described in “Materials and Methods.” Data are shown as the mean 6 SD of three independent experiments. *P , 0.05 vs control-shRNA. (e) The subcellular fractionation of the control-shRNA and CRT- shRNA2 cell lysates was conducted via discontinuous sucrose density-gradient centrifugation. The cell lysates were separated into 12 fractions (F), as described in “Materials and Methods.” The expression levels of E-cadherin, Na+/K+ ATPase (cell surface), TGN46 (trans-Golgi), GM130 (cis- Golgi), CNX, CRT, and BiP (ER) were examined in the control-shRNA and CRT-shRNA2 cells, using immunoblot analysis and specific antibodies (fractions 2 to 3; trans-Golgi; fractions 4 to 6, plasma membrane; fractions 8 to 10, cis-Golgi; fractions 9 to 12, ER).

Article Snippet: The primary antibodies used in this study are as follows: anti-CRT antibodies [Stressgen, San Diego, CA; RRID: AB_ 10618853 (25) and Abcam, Cambridge, United Kingdom; RRID: AB_447253 (26)], anti–cytokeratin (CK) 7 antibody [Dako, Glostrup, Denmark; RRID: AB_2134589 (27)], antiCD34 antibody [Dako; RRID: AB_2063006 (28)], anti-mouse isotype IgG1 antibody [Cell Signaling Technology, Danvers, MA; RRID: AB_10829607 (29)], anti–immunoglobulin-binding protein (BiP) antibody [Santa Cruz Biotechnology, Dallas, TX; RRID: AB_2119994 (30)], anti-calnexin (CNX) antibody [Stressgen; RRID: AB_10616095 (31)], anti–ER-resident protein 57 (ERp57) antibody [Stressgen; RRID: AB_10616507 (32)], anti–E-cadherin antibody [BD Biosciences, Franklin Lakes, NJ; RRID:AB_397580 (33)], anti–b-catenin antibody [Sigma-Aldrich, St. Louis, MO; RRID: AB_476831 (34)], anti–glyceraldehyde3-phosphate dehydrogenase (GAPDH) antibody [Millipore, Burlington, MA; RRID: AB_2107445 (35)], anti–Golgi matrix protein of 130 kDa (GM130) antibody [Abcam; RRID: AB_ 880266 (36)], anti–trans-Golgi network of 46 kDa (TGN46) antibody [Novus Biologicals, Centennial, CO; RRID: AB_ 10011761 (37)], and anti–Na+/K+ ATPase antibody [Thermo Fisher Scientific, Rockford, IL; RRID: AB_2060976 (38)].

Techniques: Knockdown, Expressing, Control, shRNA, Immunofluorescence, Microscopy, Staining, Marker, Avidin-Biotin Assay, Fractionation, Gradient Centrifugation, Western Blot, Clinical Proteomics, Membrane