Structured Review

Santa Cruz Biotechnology fak sirna
(A and B) HBMEC were pre-incubated with indicated concentrations of the specific <t>FAK</t> inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial <t>siRNA</t> specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.
Fak 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
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1) Product Images from "Cell Invasion by Neisseria meningitidis Requires a Functional Interplay between the Focal Adhesion Kinase, Src and Cortactin"

Article Title: Cell Invasion by Neisseria meningitidis Requires a Functional Interplay between the Focal Adhesion Kinase, Src and Cortactin

Journal: PLoS ONE

doi: 10.1371/journal.pone.0039613

(A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.
Figure Legend Snippet: (A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.

Techniques Used: Incubation, Infection, SDS Page, Transfection, Concentration Assay, Expressing, Mutagenesis


Structured Review

Santa Cruz Biotechnology fak sirna
(A and B) HBMEC were pre-incubated with indicated concentrations of the specific <t>FAK</t> inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial <t>siRNA</t> specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.
Fak 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
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1) Product Images from "Cell Invasion by Neisseria meningitidis Requires a Functional Interplay between the Focal Adhesion Kinase, Src and Cortactin"

Article Title: Cell Invasion by Neisseria meningitidis Requires a Functional Interplay between the Focal Adhesion Kinase, Src and Cortactin

Journal: PLoS ONE

doi: 10.1371/journal.pone.0039613

(A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.
Figure Legend Snippet: (A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.

Techniques Used: Incubation, Infection, SDS Page, Transfection, Concentration Assay, Expressing, Mutagenesis


Structured Review

Santa Cruz Biotechnology anti p eif2 α
TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and <t>P-eIF2</t> α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.
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1) Product Images from "Tang-Luo-Ning, a Traditional Chinese Medicine, Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis of Schwann Cells under High Glucose Environment"

Article Title: Tang-Luo-Ning, a Traditional Chinese Medicine, Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis of Schwann Cells under High Glucose Environment

Journal: Evidence-based Complementary and Alternative Medicine : eCAM

doi: 10.1155/2017/5193548

TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and P-eIF2 α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.
Figure Legend Snippet: TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and P-eIF2 α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.

Techniques Used: Expressing, High Content Screening, Western Blot


Structured Review

Santa Cruz Biotechnology human fak shrna lentiviral particles
ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant <t>shRNA</t> (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a <t>lentiviral</t> vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).
Human Fak Shrna Lentiviral Particles, supplied by Santa Cruz Biotechnology, 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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1) Product Images from "Crosstalks between integrin alpha 5 and IGF2/IGFBP2 signalling trigger human bone marrow-derived mesenchymal stromal osteogenic differentiation"

Article Title: Crosstalks between integrin alpha 5 and IGF2/IGFBP2 signalling trigger human bone marrow-derived mesenchymal stromal osteogenic differentiation

Journal: BMC Cell Biology

doi: 10.1186/1471-2121-11-44

ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant shRNA (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a lentiviral vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).
Figure Legend Snippet: ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant shRNA (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a lentiviral vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

Techniques Used: Expressing, Transduction, shRNA, Quantitative RT-PCR, Plasmid Preparation

Inhibition of ITGA5-Induced Signalling Abrogates IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs transduced with a lentiviral vector encoding ITGA5 or treated with the agonist peptide (CRRETAWAC; 100 μg/ml), and control cells were transiently transfected with a specific shRNA targeting FAK. Total RNA was collected and used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were treated with the MEK inhibitor U0126 (10 μM), or the PI3K inhibitor wortmannin (50 nM) for 24 hours and IGF2 and IGFBP2 mRNA levels were determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).
Figure Legend Snippet: Inhibition of ITGA5-Induced Signalling Abrogates IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs transduced with a lentiviral vector encoding ITGA5 or treated with the agonist peptide (CRRETAWAC; 100 μg/ml), and control cells were transiently transfected with a specific shRNA targeting FAK. Total RNA was collected and used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were treated with the MEK inhibitor U0126 (10 μM), or the PI3K inhibitor wortmannin (50 nM) for 24 hours and IGF2 and IGFBP2 mRNA levels were determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

Techniques Used: Inhibition, Expressing, Transduction, Plasmid Preparation, Transfection, shRNA, Quantitative RT-PCR


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Santa Cruz Biotechnology pmdm2
( A ) Immunoblot analysis of <t>pMdm2</t> Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.
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1) Product Images from "Vapor of Volatile Oils from Litsea cubeba Seed Induces Apoptosis and Causes Cell Cycle Arrest in Lung Cancer Cells"

Article Title: Vapor of Volatile Oils from Litsea cubeba Seed Induces Apoptosis and Causes Cell Cycle Arrest in Lung Cancer Cells

Journal: PLoS ONE

doi: 10.1371/journal.pone.0047014

( A ) Immunoblot analysis of pMdm2 Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.
Figure Legend Snippet: ( A ) Immunoblot analysis of pMdm2 Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.

Techniques Used: Western Blot, Transfection, Binding Assay, Immunoprecipitation, BrdU Incorporation Assay, Microscopy


Structured Review

Santa Cruz Biotechnology fak sirna
Fak 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
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Santa Cruz Biotechnology antibodies against fak
Antibodies Against Fak, 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
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Santa Cruz Biotechnology focal adhesion kinase fak sirna
A , Expression of <t>FAK</t> mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK <t>siRNA.</t> Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.
Focal Adhesion Kinase Fak Sirna, supplied by Santa Cruz Biotechnology, 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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1) Product Images from "Myocardial Cytoskeletal Adaptations in Advanced Kidney Disease"

Article Title: Myocardial Cytoskeletal Adaptations in Advanced Kidney Disease

Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

doi: 10.1161/JAHA.121.022991

A , Expression of FAK mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK siRNA. Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.
Figure Legend Snippet: A , Expression of FAK mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK siRNA. Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.

Techniques Used: Expressing, Ex Vivo, Real-time Polymerase Chain Reaction, Western Blot, Transfection, Filtration


Structured Review

Santa Cruz Biotechnology fak sirna
A. Western blot analysis showing that activation of <t>FAK</t> signal pathway was attenuated by knockdown of FAK by <t>siRNA</t> in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).
Fak Sirna, supplied by Santa Cruz Biotechnology, 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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1) Product Images from "G9a promotes invasion and metastasis of non-small cell lung cancer through enhancing focal adhesion kinase activation via NF-κB signaling pathway"

Article Title: G9a promotes invasion and metastasis of non-small cell lung cancer through enhancing focal adhesion kinase activation via NF-κB signaling pathway

Journal: Molecular cancer research : MCR

doi: 10.1158/1541-7786.MCR-20-0557

A. Western blot analysis showing that activation of FAK signal pathway was attenuated by knockdown of FAK by siRNA in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).
Figure Legend Snippet: A. Western blot analysis showing that activation of FAK signal pathway was attenuated by knockdown of FAK by siRNA in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).

Techniques Used: Western Blot, Activation Assay, Migration, Transfection, Plasmid Preparation


Structured Review

Santa Cruz Biotechnology fak sirna
A. Western blot analysis showing that activation of <t>FAK</t> signal pathway was attenuated by knockdown of FAK by <t>siRNA</t> in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).
Fak 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
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1) Product Images from "G9a promotes invasion and metastasis of non-small cell lung cancer through enhancing focal adhesion kinase activation via NF-κB signaling pathway"

Article Title: G9a promotes invasion and metastasis of non-small cell lung cancer through enhancing focal adhesion kinase activation via NF-κB signaling pathway

Journal: Molecular cancer research : MCR

doi: 10.1158/1541-7786.MCR-20-0557

A. Western blot analysis showing that activation of FAK signal pathway was attenuated by knockdown of FAK by siRNA in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).
Figure Legend Snippet: A. Western blot analysis showing that activation of FAK signal pathway was attenuated by knockdown of FAK by siRNA in G9a-overexpressed NSCLC cells. B. Representative images of scratch assays. 0h and 24h/ 36h for the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 / A549 upon knockdown of FAK by its specific siRNA, respectively. C. Quantitative analysis of migration distances in the control and G9a-overexpressed A549 and H1299 cells after FAK is attenuated by its specific siRNA. D. Representative images for Matrigel transwell invasion assays of the controls (pcDNA 3.1) and G9a-overexpressed (G9a-pcDNA 3.1) H1299 and A549 transfected with control and FAK siRNA. E. Quantitative analysis for invasive cells in the controls and G9a-overexpressed A549 and H1299 cancer cells upon knockdown of FAK. Data are presented as percentages of the control cells transfected with the empty plasmid pcDNA 3.1 (* P < 0.05, ** P < 0.01, *** P < 0.001, NS represents for no significance; compared to the controls cells).

Techniques Used: Western Blot, Activation Assay, Migration, Transfection, Plasmid Preparation

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    Santa Cruz Biotechnology fak sirna
    (A and B) HBMEC were pre-incubated with indicated concentrations of the specific <t>FAK</t> inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial <t>siRNA</t> specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.
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    Santa Cruz Biotechnology anti p eif2 α
    TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and <t>P-eIF2</t> α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.
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    Santa Cruz Biotechnology human fak shrna lentiviral particles
    ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant <t>shRNA</t> (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a <t>lentiviral</t> vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).
    Human Fak Shrna Lentiviral Particles, supplied by Santa Cruz Biotechnology, 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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    Santa Cruz Biotechnology pmdm2
    ( A ) Immunoblot analysis of <t>pMdm2</t> Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.
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    Santa Cruz Biotechnology antibodies against fak
    ( A ) Immunoblot analysis of <t>pMdm2</t> Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.
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    Santa Cruz Biotechnology focal adhesion kinase fak sirna
    A , Expression of <t>FAK</t> mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK <t>siRNA.</t> Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.
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    (A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.

    Journal: PLoS ONE

    Article Title: Cell Invasion by Neisseria meningitidis Requires a Functional Interplay between the Focal Adhesion Kinase, Src and Cortactin

    doi: 10.1371/journal.pone.0039613

    Figure Lengend Snippet: (A and B) HBMEC were pre-incubated with indicated concentrations of the specific FAK inhibitor PF573228 and infected for 4 h and 8 h with the unencapsulated N. meningitidis strain MC58 siaD . Intracellular bacteria were defined by gentamicin protection assay. The graph shows mean values +/− S.D. of three independent experiments done in duplicate. ** P <0.01, relative to cells infected without inhibitor. (C) HBMEC were pre-incubated with the indicated concentrations of the FAK inhibitor PF 573228 for 1 h and infected with N. meningitidis MC58 siaD for 4 h. Cell lysates were resolved by SDS-PAGE and blotted with α-phospho-FAK Tyr 397 demonstrating that PF 573228 blocked FAK Tyr 397 phosphorylation in a dose-dependent manner. (D) 293T cells were transfected with indicated concentration of a commercial siRNA specific for FAK to limit FAK protein expression or transfected with unspecific control siRNA. siRNA transfected cells were infected with mutant strain MC58 siaD and internalized bacteria were measured by gentamicin protection assay at 4 h p.i. The graph represents mean values ± S.D. of three independent experiments done in duplicate. * P <0.05 and ** P <0.01, relative to cells transfected with the control siRNA.

    Article Snippet: Validated FAK siRNA (sc-35353) was synthesized by Santa Cruz Biotechnology.

    Techniques: Incubation, Infection, SDS Page, Transfection, Concentration Assay, Expressing, Mutagenesis

    TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and P-eIF2 α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Tang-Luo-Ning, a Traditional Chinese Medicine, Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis of Schwann Cells under High Glucose Environment

    doi: 10.1155/2017/5193548

    Figure Lengend Snippet: TLN can decrease the expression of GADD34 and Ero1α and increase the expression of P-eIF2α in high glucose-induced RSC96 cells. (a) Images of GADD34 relative protein level measured by high content analysis; images were viewed at a magnification of 10x. (b) Images of Ero1 α and P-eIF2 α relative protein level measured by Western blot, normalized to β -actin. ((c)–(e)) Summarized data of GADD34, Ero1 α , and P-eIF2 α , normalized as fold change of 25 mM glucose group. Data were analyzed by one-way ANOVA followed by least significant difference. Data were shown as mean ± SEM ( n = 4). ★★ P < 0.01 and ★ P < 0.05 versus 25 mM glucose; ☆☆ P < 0.01 and ☆ P < 0.05 versus 150 mM glucose.

    Article Snippet: The following primary antibodies were used: mouse monoclonal anti-Ero1 α (1 : 500, Santa Cruz, sc-100805); rabbit polyclonal anti-IRE1 α (1 : 2000, Santa Cruz, sc-20790), anti-P-IRE1 α (1 : 2000, Abcam, ab48187), and anti-P-eIF2 α (1 : 1500, Santa Cruz, sc-293100).

    Techniques: Expressing, High Content Screening, Western Blot

    ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant shRNA (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a lentiviral vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

    Journal: BMC Cell Biology

    Article Title: Crosstalks between integrin alpha 5 and IGF2/IGFBP2 signalling trigger human bone marrow-derived mesenchymal stromal osteogenic differentiation

    doi: 10.1186/1471-2121-11-44

    Figure Lengend Snippet: ITGA5 Controls IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs were transduced with shITGA5, shITGB1 or a non relevant shRNA (shNR), total RNA was used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were transduced with a lentiviral vector encoding ITGA5, or treated with the agonist peptide CRRETAWAC (100 μg/ml) (CRRETAWAC) or with a non relevant control peptide (GRGESP; 100 μg/ml), or with a conformation-dependent anti-α5 monoclonal antibody (SNAKA51; 10 μg/ml), and IGF2 and IGFBP2 mRNA expression was determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

    Article Snippet: Non relevant shRNA (scrambled sequence that does not lead to specific degradation of any known cellular mRNA), ITGB1 shRNA and human FAK shRNA lentiviral particles (mixtures of viral particles containing 3 target-specific constructs that encode shRNA designed to knock down gene expression) were obtained from Santa Cruz Biotechnology (Heidelberg, Germany).

    Techniques: Expressing, Transduction, shRNA, Quantitative RT-PCR, Plasmid Preparation

    Inhibition of ITGA5-Induced Signalling Abrogates IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs transduced with a lentiviral vector encoding ITGA5 or treated with the agonist peptide (CRRETAWAC; 100 μg/ml), and control cells were transiently transfected with a specific shRNA targeting FAK. Total RNA was collected and used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were treated with the MEK inhibitor U0126 (10 μM), or the PI3K inhibitor wortmannin (50 nM) for 24 hours and IGF2 and IGFBP2 mRNA levels were determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

    Journal: BMC Cell Biology

    Article Title: Crosstalks between integrin alpha 5 and IGF2/IGFBP2 signalling trigger human bone marrow-derived mesenchymal stromal osteogenic differentiation

    doi: 10.1186/1471-2121-11-44

    Figure Lengend Snippet: Inhibition of ITGA5-Induced Signalling Abrogates IGF2/IGFBP2 Expression in hMSCs . Adult hMSCs transduced with a lentiviral vector encoding ITGA5 or treated with the agonist peptide (CRRETAWAC; 100 μg/ml), and control cells were transiently transfected with a specific shRNA targeting FAK. Total RNA was collected and used for quantitative RT-PCR analysis of IGF2 ( A ) and IGFBP2 ( B ). Adult hMSCs were treated with the MEK inhibitor U0126 (10 μM), or the PI3K inhibitor wortmannin (50 nM) for 24 hours and IGF2 and IGFBP2 mRNA levels were determined by quantitative RT-PCR analysis ( C-D ). Results are expressed as mean ± SD of treated over control ratio after normalization to 18 S expression. *: significant difference with untreated cells ( P <0.05).

    Article Snippet: Non relevant shRNA (scrambled sequence that does not lead to specific degradation of any known cellular mRNA), ITGB1 shRNA and human FAK shRNA lentiviral particles (mixtures of viral particles containing 3 target-specific constructs that encode shRNA designed to knock down gene expression) were obtained from Santa Cruz Biotechnology (Heidelberg, Germany).

    Techniques: Inhibition, Expressing, Transduction, Plasmid Preparation, Transfection, shRNA, Quantitative RT-PCR

    ( A ) Immunoblot analysis of pMdm2 Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.

    Journal: PLoS ONE

    Article Title: Vapor of Volatile Oils from Litsea cubeba Seed Induces Apoptosis and Causes Cell Cycle Arrest in Lung Cancer Cells

    doi: 10.1371/journal.pone.0047014

    Figure Lengend Snippet: ( A ) Immunoblot analysis of pMdm2 Ser 166 , p21 and p53 was analyzed in control or VCO exposed A549 cells at indicated time periods. β-actin used as internal loading control. ( B ) Immunoblot showed p21 level in p53 siRNA or Sp1 siRNA or their control siRNA transfected A549 cells exposed with or without VCO. ( C ) ChIP assay demonstrated VCO exposure increases binding of p53 to its response element (RE1 and RE2) on p21 promoter. ( D ) Cyclin D1-p21 interaction was increased with increasing the time of VCO exposure, which was shown by co-immunoprecipitation study. ( E ) BrdU incorporation in control and VCO treated A549 cells were examined by florescence microscopy. ( F ) FACS analysis showed cell cycle arrest at G1 to S phase as indicated by increased percentage of G 0 /G 1 cells with the decrease of S and G 2 /M phase cells. Bar represents 20 µm.

    Article Snippet: The primary antibodies for pAkt (Thr308; sc-135650), pAkt1/2/3 (Ser473; sc-7985-R), Akt 1/2/3 (sc-8312), pPDK1 (Ser241; sc-101775), Bcl-xL (sc-7195), pBad (Ser136; sc-7999), Bad (sc-7869), pMdm2 (Ser166; sc-293105), p53 (sc-6243), p21 (sc-756), cyclin D1 (sc-753), poly[ADP-ribosyl]-polymerase (PARP) (sc-7150), Cytochrome c (sc- 7159) and β-actin (sc-130657) were purchased from Santa Cruz Biotechnology Inc., California, USA and mTOR (#2983) was procured from Cell Signaling Technology Inc., Danvers, MA, USA.

    Techniques: Western Blot, Transfection, Binding Assay, Immunoprecipitation, BrdU Incorporation Assay, Microscopy

    A , Expression of FAK mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK siRNA. Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    Article Title: Myocardial Cytoskeletal Adaptations in Advanced Kidney Disease

    doi: 10.1161/JAHA.121.022991

    Figure Lengend Snippet: A , Expression of FAK mRNA is significantly upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Analysis of FAK mRNA expression by quantitative polymerase chain reaction revealed that FAK was significantly upregulated in hearts from patients undergoing hemodialysis. However, FAK mRNA expression was suppressed in hearts from patients with HTN. B , Expression of FAK protein is upregulated in left ventricular tissues from patients undergoing hemodialysis, ex vivo. Protein expression of FAK was significantly upregulated in hearts from patients undergoing hemodialysis as assessed by immunoblotting. FAK protein expression was significantly suppressed in HTN hearts. C , FAK silencing mediates cytoskeletal dysfunction in the presence of mineral stressors. (i) Primary human ventricular cardiac fibroblasts were transfected once with either scrambled or FAK siRNA. Cells were then treated daily with or without mineral stressors (ie P+Ca: 2 mmol/L β‐glycerophosphate with 1 unit/mL alkaline phosphatase, and 2.7 mmol/L calcium chloride) for 5 days. After treatment, target cytoskeletal proteins were assessed by immunoblotting. (ii) Treatment with FAK siRNA significantly reduced full‐length FAK expression at 5 days, and exposure to high calcium and high phosphate further reduced FAK expression. High calcium and high phosphate treatment resulted in detection of 80 kDa N‐terminal FAK fragment, which was decreased in combined FAK siRNA and high mineral stressors treatment. There was no statistical difference in FAK expression between the control and scrambled siRNA groups. (iii) There was no significant difference in β‐actin expression across the groups. (iv) β‐Tubulin was significantly decreased in cardiac fibroblasts exposed to mineral stressors compared with controls, but was not significantly different in the FAK silencing groups. (v) Vimentin was decreased significantly when cardiac fibroblasts were exposed to high calcium and high phosphate, and further decreased in the FAK silenced group exposed to high calcium and high phosphate. (vi) Expression of vinculin followed a similar pattern to vimentin. D , Schematic diagram of ultrastructural adaptations of the failing myocardium in CKD. In the healthy individuals, interactions between the heart and kidney is critical for normal physiological function. Patients with advanced CKD on hemodialysis (HD) exhibited significant cytoskeletal maladaptations that were generally more severe than hypertensive control hearts. HD hearts exhibited a unique pattern of severely reduced β‐actin, β‐tubulin and upregulation of vinculin expression. Cytoskeletal dysregulation in HD and HTN hearts is associated with mitochondrial dysfunction (reduced OPA1 and MFN1 genes responsible for mitochondrial fusion and division) and loss of cell survival pathways. FAK is a cytosolic tyrosine kinase that plays a central role in regulating cytoskeletal integrity. FAK expression is upregulated in HD hearts. This may account for increased expression of anchor protein vinculin observed as a protective response. GFR indicates glomerular filtration rate.

    Article Snippet: Human ventricular cardiac fibroblasts were serum starved for 24 hours prior to transfection with either focal adhesion kinase (FAK) siRNA (Cat. No. sc‐29310; Santa Cruz Biotechnology, Dallas, TX) or siRNA‐B (Cat. No. sc‐44230; Santa Cruz Biotechnology, Dallas, TX).

    Techniques: Expressing, Ex Vivo, Real-time Polymerase Chain Reaction, Western Blot, Transfection, Filtration