p63 gene tex Search Results


rabbit polyclonal anti-p63 [n2c1]  (GeneTex)
90
GeneTex rabbit polyclonal anti-p63 [n2c1]
a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA specific to <t>p63.</t> Total RNA was extracted and ΔNp63α transcript level was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in p63 transcript levels relative to NSC-transfected cells. Immunoblots of p63 in A431 and HaCaT cells transfected are shown in the bottom panels. b TaqMan based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( a ). c H1299 and SW480 cells null for p63 were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. Transcripts were quantified by qRT-PCR (upper panel) while protein levels were confirmed using immunoblot analyses (lower panel). d Taqman based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( c ). Immunoblot with β-actin was performed to confirm equivalent protein loading. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to controls are indicated with an asterisk. e H1299 cells were co-transfected with p63-BS-Luc reporter construct along with either empty vector or increasing concentrations of ΔNp63α as indicated. Cells were subjected to dual luciferase assay at 24 h after transfection. The y -axis represents fold change in relative luciferase units (RLU) compared with cells transfected with empty vector. RLU values are shown as means ± S.E.M. from n = 3 experiments
Rabbit Polyclonal Anti P63 [N2c1], supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti-p63 [n2c1]/product/GeneTex
Average 90 stars, based on 1 article reviews
rabbit polyclonal anti-p63 [n2c1] - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
p63 antibody [4a4] mouse monoclonal  (GeneTex)
90
GeneTex p63 antibody [4a4] mouse monoclonal
a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA specific to <t>p63.</t> Total RNA was extracted and ΔNp63α transcript level was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in p63 transcript levels relative to NSC-transfected cells. Immunoblots of p63 in A431 and HaCaT cells transfected are shown in the bottom panels. b TaqMan based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( a ). c H1299 and SW480 cells null for p63 were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. Transcripts were quantified by qRT-PCR (upper panel) while protein levels were confirmed using immunoblot analyses (lower panel). d Taqman based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( c ). Immunoblot with β-actin was performed to confirm equivalent protein loading. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to controls are indicated with an asterisk. e H1299 cells were co-transfected with p63-BS-Luc reporter construct along with either empty vector or increasing concentrations of ΔNp63α as indicated. Cells were subjected to dual luciferase assay at 24 h after transfection. The y -axis represents fold change in relative luciferase units (RLU) compared with cells transfected with empty vector. RLU values are shown as means ± S.E.M. from n = 3 experiments
P63 Antibody [4a4] Mouse Monoclonal, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/p63 antibody [4a4] mouse monoclonal/product/GeneTex
Average 90 stars, based on 1 article reviews
p63 antibody [4a4] mouse monoclonal - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA specific to p63. Total RNA was extracted and ΔNp63α transcript level was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in p63 transcript levels relative to NSC-transfected cells. Immunoblots of p63 in A431 and HaCaT cells transfected are shown in the bottom panels. b TaqMan based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( a ). c H1299 and SW480 cells null for p63 were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. Transcripts were quantified by qRT-PCR (upper panel) while protein levels were confirmed using immunoblot analyses (lower panel). d Taqman based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( c ). Immunoblot with β-actin was performed to confirm equivalent protein loading. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to controls are indicated with an asterisk. e H1299 cells were co-transfected with p63-BS-Luc reporter construct along with either empty vector or increasing concentrations of ΔNp63α as indicated. Cells were subjected to dual luciferase assay at 24 h after transfection. The y -axis represents fold change in relative luciferase units (RLU) compared with cells transfected with empty vector. RLU values are shown as means ± S.E.M. from n = 3 experiments

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA specific to p63. Total RNA was extracted and ΔNp63α transcript level was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in p63 transcript levels relative to NSC-transfected cells. Immunoblots of p63 in A431 and HaCaT cells transfected are shown in the bottom panels. b TaqMan based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( a ). c H1299 and SW480 cells null for p63 were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. Transcripts were quantified by qRT-PCR (upper panel) while protein levels were confirmed using immunoblot analyses (lower panel). d Taqman based qRT-PCR was used to quantify miR-320a levels from the experiment described in ( c ). Immunoblot with β-actin was performed to confirm equivalent protein loading. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to controls are indicated with an asterisk. e H1299 cells were co-transfected with p63-BS-Luc reporter construct along with either empty vector or increasing concentrations of ΔNp63α as indicated. Cells were subjected to dual luciferase assay at 24 h after transfection. The y -axis represents fold change in relative luciferase units (RLU) compared with cells transfected with empty vector. RLU values are shown as means ± S.E.M. from n = 3 experiments

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Control, Quantitative RT-PCR, Western Blot, Plasmid Preparation, Expressing, Standard Deviation, Construct, Luciferase

a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA targeting p63. b H1299 and SW480 cells were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. The change in transcript and protein levels of Rac1 were measured by TaqMan based qRT-PCR (* indicates P ≤ 0.05) and immunoblot analysis, respectively. Error bars represent standard deviation. c A431 and HaCaT cells were transfected with nonsilencing control siRNA (NSC) or siRNA against p63. d Caco2 and SW480 cells were transfected with empty vector control or ΔNp63α and subjected to immunoblot analysis for the indicated proteins. The change in Rac1 protein expression was measured by immunoblot analysis using Rac1 and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: a A431 and HaCaT cells were transfected with non-silencing control siRNA (NSC) or siRNA targeting p63. b H1299 and SW480 cells were transfected with empty vector (EV) control or expression plasmid encoding ΔNp63α. The change in transcript and protein levels of Rac1 were measured by TaqMan based qRT-PCR (* indicates P ≤ 0.05) and immunoblot analysis, respectively. Error bars represent standard deviation. c A431 and HaCaT cells were transfected with nonsilencing control siRNA (NSC) or siRNA against p63. d Caco2 and SW480 cells were transfected with empty vector control or ΔNp63α and subjected to immunoblot analysis for the indicated proteins. The change in Rac1 protein expression was measured by immunoblot analysis using Rac1 and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Control, Plasmid Preparation, Expressing, Quantitative RT-PCR, Western Blot, Standard Deviation

A431 cells were transfected with NSC siRNA, p63 siRNA, and/or Rac1 siRNA as indicated. At 24 h after the second round of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( a ) and the number of invading cells was quantitated after 21 h ( b ). The y -axis indicates the average number of cells invaded per field. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk. c The change in protein expression was measured by immunoblot analysis using Rac1 and pRac1 (S71) antibodies to measure unphosphorylated and phosphorylated levels of Rac1, respectively. Immunoblot with β-actin was performed to confirm equivalent protein loading

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: A431 cells were transfected with NSC siRNA, p63 siRNA, and/or Rac1 siRNA as indicated. At 24 h after the second round of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( a ) and the number of invading cells was quantitated after 21 h ( b ). The y -axis indicates the average number of cells invaded per field. Error bars represent standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk. c The change in protein expression was measured by immunoblot analysis using Rac1 and pRac1 (S71) antibodies to measure unphosphorylated and phosphorylated levels of Rac1, respectively. Immunoblot with β-actin was performed to confirm equivalent protein loading

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Invasion Assay, Standard Deviation, Expressing, Western Blot

A431 cells were transfected with either non-silencing control (NSC) or sip63 in conjunction with a negative control mimic or miR-320a mimic for two rounds of transfections. a The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1, and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. Twenty four hour after the second of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( b ) and the number of invading cells was quantitated after 21 h ( c ). The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to cells transfected with NSC and control mimic are indicated with an asterisk

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: A431 cells were transfected with either non-silencing control (NSC) or sip63 in conjunction with a negative control mimic or miR-320a mimic for two rounds of transfections. a The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1, and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. Twenty four hour after the second of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( b ) and the number of invading cells was quantitated after 21 h ( c ). The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to cells transfected with NSC and control mimic are indicated with an asterisk

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Control, Negative Control, Western Blot, Invasion Assay, Standard Deviation

a A putative miR-320a binding site in PKCγ 3′UTR identified by Target Scan. b A431 cells were co-transfected with a luciferase reporter carrying PKCγ 3′UTR or a random 3′UTR along with control mimic or miR-320a mimic. At 24 h post transfection, a luciferase reporter assays were performed. y -Axis represents the relative change in the luciferase activity. Significant changes ( P ≤ 0.05) relative to control mimic are indicated with an asterisk. c HaCaT cells were transfected with either NSC siRNA or p63 siRNA in conjunction with a negative control mimic or miR-320a mimic as indicated. Total RNA was extracted and transcript levels of ΔNp63α and PKCγ was measured by Taqman based qRT-PCR (upper panel). y -Axis represents the fold change in ΔNp63α and PKCγ transcript levels relative to NSC-transfected cells. Error bars indicate standard deviation. Significant changes ( P ≤ 0.05) relative to respective NSC controls are indicated with an asterisk. The change in indicated protein levels were measured analyzed via immunoblotting with p63, PKCγ, Rac1, and pRac1 (S71) antibodies as indicated (lower panel). Immunoblot with β-actin was performed to confirm equivalent protein loading

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: a A putative miR-320a binding site in PKCγ 3′UTR identified by Target Scan. b A431 cells were co-transfected with a luciferase reporter carrying PKCγ 3′UTR or a random 3′UTR along with control mimic or miR-320a mimic. At 24 h post transfection, a luciferase reporter assays were performed. y -Axis represents the relative change in the luciferase activity. Significant changes ( P ≤ 0.05) relative to control mimic are indicated with an asterisk. c HaCaT cells were transfected with either NSC siRNA or p63 siRNA in conjunction with a negative control mimic or miR-320a mimic as indicated. Total RNA was extracted and transcript levels of ΔNp63α and PKCγ was measured by Taqman based qRT-PCR (upper panel). y -Axis represents the fold change in ΔNp63α and PKCγ transcript levels relative to NSC-transfected cells. Error bars indicate standard deviation. Significant changes ( P ≤ 0.05) relative to respective NSC controls are indicated with an asterisk. The change in indicated protein levels were measured analyzed via immunoblotting with p63, PKCγ, Rac1, and pRac1 (S71) antibodies as indicated (lower panel). Immunoblot with β-actin was performed to confirm equivalent protein loading

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Binding Assay, Transfection, Luciferase, Control, Activity Assay, Negative Control, Quantitative RT-PCR, Standard Deviation, Western Blot

A431 cells were transfected with either non-silencing control (NSC), sip63 alone, siPKCγ alone, or sip63 in conjugation with siPKCγ for two rounds of transfections. a At 24 h post transfection, the change in transcript levels of PKCγ was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in PKCγ transcript levels relative to NSC-transfected cells. Error bars represent standard deviation. b The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1 and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. c Quantification of pRac1 levels. Relative protein values are shown as means ± S.E.M. from n = 3 experiments. Twenty four hour after the second round of transfection, 8.0 × 104 cells were subjected to Matrigel-based invasion assay ( d ) and the number of invading cells was quantitated after 21 h ( e ). The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: A431 cells were transfected with either non-silencing control (NSC), sip63 alone, siPKCγ alone, or sip63 in conjugation with siPKCγ for two rounds of transfections. a At 24 h post transfection, the change in transcript levels of PKCγ was measured by TaqMan based qRT-PCR. y -Axis represents the fold change in PKCγ transcript levels relative to NSC-transfected cells. Error bars represent standard deviation. b The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1 and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. c Quantification of pRac1 levels. Relative protein values are shown as means ± S.E.M. from n = 3 experiments. Twenty four hour after the second round of transfection, 8.0 × 104 cells were subjected to Matrigel-based invasion assay ( d ) and the number of invading cells was quantitated after 21 h ( e ). The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Control, Conjugation Assay, Quantitative RT-PCR, Standard Deviation, Western Blot, Invasion Assay

A431 cells were transfected with either NSC siRNA or siRNA targeting p63 for two rounds of transfections followed by treatment with DMSO or Gӧ6976 for 2 h as indicated. a The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1, and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. b The fold change in pRac1 levels relative to NSC DMSO-treated cells levels. Relative protein values are shown as means ± S.E.M. from n = 3 experiments. c At 24 h after the second round of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( c ) and the number of invading cells was quantitated after 21 h. d The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk. e A431 cells were incubated with DMSO or 100 nM of PMA for the indicated times. The change in indicated protein levels were analyzed via immunoblotting with Rac1 and pRac1 (S71) antibodies as indicated. f A431 cells were treated with DMSO or Gö6976 for 2 h and followed by incubation with 100 nM of PMA for 15 min. The change in indicated protein levels were analyzed via immunoblotting as indicated. g A431 cells were transfected with nonsilencing control siRNA (NSC) or siRNA specific to PKCγ followed by treatment with DMSO or 100 nM PMA for 15 min. Total RNA was extracted and transcript levels of PKCγ was analyzed by qRT-PCR. y -Axis represents the fold change in PKCγ transcript levels relative to NSC-transfected cells. The change in Rac1 and pRac1 levels was measured by immunoblot analysis ( h ). Immunoblot with β-actin was performed to confirm equivalent protein loading

Journal: Cell Death & Disease

Article Title: ΔNp63α suppresses cells invasion by downregulating PKCγ/Rac1 signaling through miR-320a

doi: 10.1038/s41419-019-1921-6

Figure Lengend Snippet: A431 cells were transfected with either NSC siRNA or siRNA targeting p63 for two rounds of transfections followed by treatment with DMSO or Gӧ6976 for 2 h as indicated. a The change in indicated protein levels were analyzed via immunoblotting with p63, Rac1, and pRac1 (S71) antibodies as indicated. Immunoblot with β-actin was performed to confirm equivalent protein loading. b The fold change in pRac1 levels relative to NSC DMSO-treated cells levels. Relative protein values are shown as means ± S.E.M. from n = 3 experiments. c At 24 h after the second round of transfection, 8.0 × 10 4 cells were subjected to Matrigel-based invasion assay ( c ) and the number of invading cells was quantitated after 21 h. d The y -axis indicates the average number of cells invaded per field +1 standard deviation. Significant changes ( P ≤ 0.05) relative to NSC controls are indicated with an asterisk. e A431 cells were incubated with DMSO or 100 nM of PMA for the indicated times. The change in indicated protein levels were analyzed via immunoblotting with Rac1 and pRac1 (S71) antibodies as indicated. f A431 cells were treated with DMSO or Gö6976 for 2 h and followed by incubation with 100 nM of PMA for 15 min. The change in indicated protein levels were analyzed via immunoblotting as indicated. g A431 cells were transfected with nonsilencing control siRNA (NSC) or siRNA specific to PKCγ followed by treatment with DMSO or 100 nM PMA for 15 min. Total RNA was extracted and transcript levels of PKCγ was analyzed by qRT-PCR. y -Axis represents the fold change in PKCγ transcript levels relative to NSC-transfected cells. The change in Rac1 and pRac1 levels was measured by immunoblot analysis ( h ). Immunoblot with β-actin was performed to confirm equivalent protein loading

Article Snippet: Proteins were detected using the following antibodies: rabbit polyclonal anti-p63 [N2C1] (Gene Tex, Irvine, CA, USA), mouse monoclonal anti-Rac1 [23A8] (Abcam, Cambridge, MA, USA), rabbit polyclonal anti-Rac1 (C-11), rabbit polyclonal anti-phospho-Rac1 (Ser71), mouse monoclonal anti-β-actin antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA), and rabbit polyclonal anti-PKCγ (ABclonal Science, Woburn, MA, USA).

Techniques: Transfection, Western Blot, Invasion Assay, Standard Deviation, Incubation, Control, Quantitative RT-PCR