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pkcγ sirna  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology pkcγ sirna
Figure 3: PLC𝛄1 regulation in plasma membrane translocation of Hsp90𝛂. A) Signaling pathways regulating membrane translocation of Hsp90α were screened using inhibitors of PLC, PI3K, Src and Erk. Cell-surface expression of Hsp90α was detected by confocal imaging. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 50 μm. B) Plasma membrane extractions of tumor cells pretreated with the inhibitors of PLC, PI3K, Src and Erk were separated with 12% SDS–PAGE and blotted with anti-Hsp90α antibody. C) Activation of PLCγ1 was detected after treating the cells with the PLC inhibitor U73122 (PLCi). D) Immunofluorescence analysis of cell-surface Hsp90α by confocal imaging, on cells treated with PLCγ1 <t>siRNA.</t> Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 100 μm. E) Membrane extraction of tumor cells pretreated with PLCγ1 siRNA was detected by western blotting with anti-Hsp90α antibody. F) Cells were pretreated with PLCγ1 siRNA. Lysates were immunoprecipitated with anti-Hsp90α antibody. Western blotting analyses of IP samples were performed using a phospho-Thr mouse mAb. G) Levels of plasma membrane Hsp90α and total PLCγ1 in lysates of MDA-MB-231 and SKBr-3 cells were detected by western blotting.
Pkcγ Sirna, supplied by Santa Cruz Biotechnology, 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/product/pkc%CE%B3+sirna/pm24899266-305-0-5?v=Santa+Cruz+Biotechnology
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pkcγ sirna - by Bioz Stars, 2026-07
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pkc gamma prkcg human sirna oligo duplex  (OriGene)
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PRKCG Human 3 unique 27mer siRNA duplexes 2 nmol each
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Figure 3: PLC𝛄1 regulation in plasma membrane translocation of Hsp90𝛂. A) Signaling pathways regulating membrane translocation of Hsp90α were screened using inhibitors of PLC, PI3K, Src and Erk. Cell-surface expression of Hsp90α was detected by confocal imaging. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 50 μm. B) Plasma membrane extractions of tumor cells pretreated with the inhibitors of PLC, PI3K, Src and Erk were separated with 12% SDS–PAGE and blotted with anti-Hsp90α antibody. C) Activation of PLCγ1 was detected after treating the cells with the PLC inhibitor U73122 (PLCi). D) Immunofluorescence analysis of cell-surface Hsp90α by confocal imaging, on cells treated with PLCγ1 siRNA. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 100 μm. E) Membrane extraction of tumor cells pretreated with PLCγ1 siRNA was detected by western blotting with anti-Hsp90α antibody. F) Cells were pretreated with PLCγ1 siRNA. Lysates were immunoprecipitated with anti-Hsp90α antibody. Western blotting analyses of IP samples were performed using a phospho-Thr mouse mAb. G) Levels of plasma membrane Hsp90α and total PLCγ1 in lysates of MDA-MB-231 and SKBr-3 cells were detected by western blotting.

Journal: Traffic (Copenhagen, Denmark)

Article Title: PLCγ1-PKCγ signaling-mediated Hsp90α plasma membrane translocation facilitates tumor metastasis.

doi: 10.1111/tra.12179

Figure Lengend Snippet: Figure 3: PLC𝛄1 regulation in plasma membrane translocation of Hsp90𝛂. A) Signaling pathways regulating membrane translocation of Hsp90α were screened using inhibitors of PLC, PI3K, Src and Erk. Cell-surface expression of Hsp90α was detected by confocal imaging. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 50 μm. B) Plasma membrane extractions of tumor cells pretreated with the inhibitors of PLC, PI3K, Src and Erk were separated with 12% SDS–PAGE and blotted with anti-Hsp90α antibody. C) Activation of PLCγ1 was detected after treating the cells with the PLC inhibitor U73122 (PLCi). D) Immunofluorescence analysis of cell-surface Hsp90α by confocal imaging, on cells treated with PLCγ1 siRNA. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 100 μm. E) Membrane extraction of tumor cells pretreated with PLCγ1 siRNA was detected by western blotting with anti-Hsp90α antibody. F) Cells were pretreated with PLCγ1 siRNA. Lysates were immunoprecipitated with anti-Hsp90α antibody. Western blotting analyses of IP samples were performed using a phospho-Thr mouse mAb. G) Levels of plasma membrane Hsp90α and total PLCγ1 in lysates of MDA-MB-231 and SKBr-3 cells were detected by western blotting.

Article Snippet: PKCγ siRNA was purchased from Santa Cruz.

Techniques: Clinical Proteomics, Membrane, Translocation Assay, Protein-Protein interactions, Expressing, Imaging, SDS Page, Activation Assay, Extraction, Western Blot, Immunoprecipitation

Figure 4: PKC𝛄mediation of PLC𝛄1’s function in regulating cell plasma membrane translocation of Hsp90𝛂. A) Western blotting analysis of plasma membrane Hsp90α after cells were treated with different doses of the intracellular Ca2+ chelator BAPTA-AM. B) Membrane Hsp90α was detected by western blotting analysis of cells treated with the PKC inhibitor chelerythrine chloride (100 nM, 1 μM) or activator PMA (100 nM, 1 μM). C) Cells were pretreated with PLC inhibitor or PKC inhibitor, and then EGF was added. Lysates were immunoprecipitated with anti-Hsp90α antibody. Western blotting analyses of IP samples were performed using a phospho-Thr mouse mAb. D) Representative images of membrane translocation of Hsp90α in MDA-MB-231 cells. Cell-surface Hsp90α was detected by confocal imaging. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 100 μm. E) Analysis of membrane-localized Hsp90α in cells transduced with PKCγ siRNA or PKCγ plasmid; 48 h after treatment, cell lysates and plasma membrane extracts were analyzed by western blotting. Scramble RNA or vector was used as negative controls for siRNA or plasmid experiments, respectively. F) Cells transduced with PKCγ siRNA or PKCγ plasmid; 48 h after treatment, cell lysates were detected. G) Analysis of membrane Hsp90α after treatment with Rab11 siRNA (Rab11A and Rab11B). Scramble RNA was used as the control. H) Levels of Hsp90α in plasma membranes were detected by western blotting after cells were treated with Rab11 siRNA and PKCγ plasmid.

Journal: Traffic (Copenhagen, Denmark)

Article Title: PLCγ1-PKCγ signaling-mediated Hsp90α plasma membrane translocation facilitates tumor metastasis.

doi: 10.1111/tra.12179

Figure Lengend Snippet: Figure 4: PKC𝛄mediation of PLC𝛄1’s function in regulating cell plasma membrane translocation of Hsp90𝛂. A) Western blotting analysis of plasma membrane Hsp90α after cells were treated with different doses of the intracellular Ca2+ chelator BAPTA-AM. B) Membrane Hsp90α was detected by western blotting analysis of cells treated with the PKC inhibitor chelerythrine chloride (100 nM, 1 μM) or activator PMA (100 nM, 1 μM). C) Cells were pretreated with PLC inhibitor or PKC inhibitor, and then EGF was added. Lysates were immunoprecipitated with anti-Hsp90α antibody. Western blotting analyses of IP samples were performed using a phospho-Thr mouse mAb. D) Representative images of membrane translocation of Hsp90α in MDA-MB-231 cells. Cell-surface Hsp90α was detected by confocal imaging. Actin filaments (red), Hsp90α on the cell surface (green) and DAPI (blue). Scale bar: 100 μm. E) Analysis of membrane-localized Hsp90α in cells transduced with PKCγ siRNA or PKCγ plasmid; 48 h after treatment, cell lysates and plasma membrane extracts were analyzed by western blotting. Scramble RNA or vector was used as negative controls for siRNA or plasmid experiments, respectively. F) Cells transduced with PKCγ siRNA or PKCγ plasmid; 48 h after treatment, cell lysates were detected. G) Analysis of membrane Hsp90α after treatment with Rab11 siRNA (Rab11A and Rab11B). Scramble RNA was used as the control. H) Levels of Hsp90α in plasma membranes were detected by western blotting after cells were treated with Rab11 siRNA and PKCγ plasmid.

Article Snippet: PKCγ siRNA was purchased from Santa Cruz.

Techniques: Clinical Proteomics, Membrane, Translocation Assay, Western Blot, Immunoprecipitation, Imaging, Transduction, Plasmid Preparation, Control