caldesmon cald1  (Cell Signaling Technology Inc)


Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon cald1
    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of <t>CALD1</t> and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm
    Caldesmon Cald1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon cald1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon cald1 - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Oligosarcomas, IDH-mutant are distinct and aggressive"

    Article Title: Oligosarcomas, IDH-mutant are distinct and aggressive

    Journal: Acta Neuropathologica

    doi: 10.1007/s00401-021-02395-z

    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm
    Figure Legend Snippet: Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm

    Techniques Used: Immunohistochemistry, Expressing

    caldesmon cald1  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon cald1
    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of <t>CALD1</t> and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm
    Caldesmon Cald1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon cald1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon cald1 - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Oligosarcomas, IDH-mutant are distinct and aggressive"

    Article Title: Oligosarcomas, IDH-mutant are distinct and aggressive

    Journal: Acta Neuropathologica

    doi: 10.1007/s00401-021-02395-z

    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm
    Figure Legend Snippet: Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm

    Techniques Used: Immunohistochemistry, Expressing

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    Antibodies Used
    Figure Legend Snippet: Antibodies Used

    Techniques Used:

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    Antibodies Used
    Figure Legend Snippet: Antibodies Used

    Techniques Used:

    caldesmon 1  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon 1
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-02
    93/100 stars

    Images

    caldesmon  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc caldesmon
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Caldesmon, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon - by Bioz Stars, 2023-02
    93/100 stars

    Images

    1) Product Images from "Nonsteroidal Anti-Inflammatory Drugs Prevent Vincristine-Dependent Cancer-Associated Fibroblasts Formation"

    Article Title: Nonsteroidal Anti-Inflammatory Drugs Prevent Vincristine-Dependent Cancer-Associated Fibroblasts Formation

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms20081941

    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Figure Legend Snippet: Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.

    Techniques Used: Cell Culture, Isolation, Western Blot

    Mesenchymal transdifferentiation in HMEC-1 is not induced by CM from colon cancer cells treated with vincristine. HMEC-1 cells were cultured in medium supplemented with CM isolated from colon cancer cell lines maintained in CM CAFs and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), and capillary assay ( n = 9) ( C ) were analyzed. In the Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3). The blots are representative of three independent experiments.
    Figure Legend Snippet: Mesenchymal transdifferentiation in HMEC-1 is not induced by CM from colon cancer cells treated with vincristine. HMEC-1 cells were cultured in medium supplemented with CM isolated from colon cancer cell lines maintained in CM CAFs and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), and capillary assay ( n = 9) ( C ) were analyzed. In the Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3). The blots are representative of three independent experiments.

    Techniques Used: Cell Culture, Isolation, Western Blot

    NSAIDs inhibit the effect of vincristine-induced EndMT stimulation. Level of TGF-βs (TGF-β1 and TGF-β2) and IL-6 in CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM treated, if necessary, with vincristine ( A ) were studied by Western blot. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments. As the control of loading, the Ponceau Staining was shown. Then, HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM and treated, if necessary, with vincristine (+VIN) or NSAIDs (IBU or AsA). Then, elongation ratio ( n = 6) ( B ), capillary assay ( n = 9) ( C ), and level of contraction protein (caldesmon, tropomyosin), vimentin, and α-SMA were analyzed by Western blot ( D ), with GAPDH used as the loading control. The results are provided as means ± SD ( n = 3), ** p < 0.001, *** p < 0.005. The blots are representative of three independent experiments. The values from control cells are marked by dashed lines.
    Figure Legend Snippet: NSAIDs inhibit the effect of vincristine-induced EndMT stimulation. Level of TGF-βs (TGF-β1 and TGF-β2) and IL-6 in CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM treated, if necessary, with vincristine ( A ) were studied by Western blot. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments. As the control of loading, the Ponceau Staining was shown. Then, HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM and treated, if necessary, with vincristine (+VIN) or NSAIDs (IBU or AsA). Then, elongation ratio ( n = 6) ( B ), capillary assay ( n = 9) ( C ), and level of contraction protein (caldesmon, tropomyosin), vimentin, and α-SMA were analyzed by Western blot ( D ), with GAPDH used as the loading control. The results are provided as means ± SD ( n = 3), ** p < 0.001, *** p < 0.005. The blots are representative of three independent experiments. The values from control cells are marked by dashed lines.

    Techniques Used: Isolation, Western Blot, Staining, Cell Culture

    anti caldesmon cald1  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc anti caldesmon cald1
    Anti Caldesmon Cald1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti caldesmon cald1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti caldesmon cald1 - by Bioz Stars, 2023-02
    93/100 stars

    Images

    anti caldesmon  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc anti caldesmon
    Anti Caldesmon, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti caldesmon/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti caldesmon - by Bioz Stars, 2023-02
    93/100 stars

    Images

    phosphorylated erk1 2  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc phosphorylated erk1 2
    Phosphorylated Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated erk1 2/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated erk1 2 - by Bioz Stars, 2023-02
    93/100 stars

    Images

    rabbit polyclonal antiee cad antibody  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93

    Structured Review

    Cell Signaling Technology Inc rabbit polyclonal antiee cad antibody
    Rabbit Polyclonal Antiee Cad Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antiee cad antibody/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antiee cad antibody - by Bioz Stars, 2023-02
    93/100 stars

    Images

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Cell Signaling Technology Inc caldesmon cald1
    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of <t>CALD1</t> and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm
    Caldesmon Cald1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon cald1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon cald1 - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc caldesmon 1
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc caldesmon
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Caldesmon, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc anti caldesmon cald1
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Anti Caldesmon Cald1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti caldesmon cald1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti caldesmon cald1 - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc anti caldesmon
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Anti Caldesmon, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti caldesmon/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti caldesmon - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc phosphorylated erk1 2
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Phosphorylated Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated erk1 2/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated erk1 2 - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc rabbit polyclonal antiee cad antibody
    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins <t>(caldesmon,</t> tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.
    Rabbit Polyclonal Antiee Cad Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antiee cad antibody/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antiee cad antibody - by Bioz Stars, 2023-02
    93/100 stars
      Buy from Supplier

    Image Search Results


    Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm

    Journal: Acta Neuropathologica

    Article Title: Oligosarcomas, IDH-mutant are distinct and aggressive

    doi: 10.1007/s00401-021-02395-z

    Figure Lengend Snippet: Oligosarcomas have a highly distinct proteome with evidence for smooth muscle differentiation. a Volcano plot of significantly differentially regulated proteins between oligosaroma and conventional grade 3 oligodendroglioma. Using the 500 most variable proteins of the dataset for principal component analysis ( b ) and unsupervised hierarchical clustering ( c ) differentiates oligosarcomas from conventional grade 3 oligodendrogliomas. d Heatmap shows upregulation of (smooth) muscle specific proteins in oligosarcomas (left) and immunohistochemistry confirms expression of CALD1 and ACTA2 (SMA) in tumor cells of oligosarcoma (right). Scale bar is 200 µm

    Article Snippet: Primary antibodies were diluted as follows: IDH1 R132H (1:2, clone H09 [ ]), NF1 (1:4, clone NFC [ ]), p53 (1:50, Novocastra, Leica, Wetzlar, Germany), SMA (1:500, Cell Marque, Sigma Aldrich, St. Louis, USA), H3K27me3 (1:25, monoclonal antibody, Cell signalling, Danvers, USA), YAP1 (1:100, Cell signalling), Caldesmon (CALD1) (1:100, clone E89, zytomed-systems, Berlin, Germany), GFAP (1:2000, clone GA5, Cell signalling, Danvers, USA), OLIG2 (1:50, clone ERP 2673, Abcam, Cambridge, UK).

    Techniques: Immunohistochemistry, Expressing

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques: Mutagenesis

    Antibodies Used

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Antibodies Used

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques:

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Article Snippet: Caldesmon-1 , Cell Signaling Technology #2980.

    Techniques: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Article Snippet: Caldesmon-1 , Cell Signaling Technology #2980.

    Techniques: Mutagenesis

    Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Nonsteroidal Anti-Inflammatory Drugs Prevent Vincristine-Dependent Cancer-Associated Fibroblasts Formation

    doi: 10.3390/ijms20081941

    Figure Lengend Snippet: Mesenchymal transdifferentiation in HMEC-1 is modulated by vincristine-treated CAF-like cells. HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer (LS180—co-CM1 or LoVo—co-CM2) or CAF-like cells maintained in CM colon cancer cells (LS180—CAFs-CM1 or LoVo—CAFs-CM2) and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), capillary assay ( n = 9) ( C ), and proliferation ability ( D ) were analyzed. In Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments.

    Article Snippet: In particular experiments, the blots were incubated with primary antibodies recognizing α-SMA, tropomyosin, caldesmon, vimentin (cell signaling), TUBA, TUBB2, TUBB3, TUBB4, GAPDH and IL-6, TGF-β1 or TGF-β2.

    Techniques: Cell Culture, Isolation, Western Blot

    Mesenchymal transdifferentiation in HMEC-1 is not induced by CM from colon cancer cells treated with vincristine. HMEC-1 cells were cultured in medium supplemented with CM isolated from colon cancer cell lines maintained in CM CAFs and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), and capillary assay ( n = 9) ( C ) were analyzed. In the Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3). The blots are representative of three independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Nonsteroidal Anti-Inflammatory Drugs Prevent Vincristine-Dependent Cancer-Associated Fibroblasts Formation

    doi: 10.3390/ijms20081941

    Figure Lengend Snippet: Mesenchymal transdifferentiation in HMEC-1 is not induced by CM from colon cancer cells treated with vincristine. HMEC-1 cells were cultured in medium supplemented with CM isolated from colon cancer cell lines maintained in CM CAFs and treated, if necessary, with vincristine (+VIN). Then, elongation ratio ( n = 6) ( A ), level of contraction proteins (caldesmon, tropomyosin), vimentin, and α-SMA (Western blot) ( B ), and capillary assay ( n = 9) ( C ) were analyzed. In the Western blot assay, GAPDH was used as the loading control. The results are provided as means ± SD ( n = 3). The blots are representative of three independent experiments.

    Article Snippet: In particular experiments, the blots were incubated with primary antibodies recognizing α-SMA, tropomyosin, caldesmon, vimentin (cell signaling), TUBA, TUBB2, TUBB3, TUBB4, GAPDH and IL-6, TGF-β1 or TGF-β2.

    Techniques: Cell Culture, Isolation, Western Blot

    NSAIDs inhibit the effect of vincristine-induced EndMT stimulation. Level of TGF-βs (TGF-β1 and TGF-β2) and IL-6 in CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM treated, if necessary, with vincristine ( A ) were studied by Western blot. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments. As the control of loading, the Ponceau Staining was shown. Then, HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM and treated, if necessary, with vincristine (+VIN) or NSAIDs (IBU or AsA). Then, elongation ratio ( n = 6) ( B ), capillary assay ( n = 9) ( C ), and level of contraction protein (caldesmon, tropomyosin), vimentin, and α-SMA were analyzed by Western blot ( D ), with GAPDH used as the loading control. The results are provided as means ± SD ( n = 3), ** p < 0.001, *** p < 0.005. The blots are representative of three independent experiments. The values from control cells are marked by dashed lines.

    Journal: International Journal of Molecular Sciences

    Article Title: Nonsteroidal Anti-Inflammatory Drugs Prevent Vincristine-Dependent Cancer-Associated Fibroblasts Formation

    doi: 10.3390/ijms20081941

    Figure Lengend Snippet: NSAIDs inhibit the effect of vincristine-induced EndMT stimulation. Level of TGF-βs (TGF-β1 and TGF-β2) and IL-6 in CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM treated, if necessary, with vincristine ( A ) were studied by Western blot. The results are provided as means ± SD ( n = 3); * p < 0.05, *** p < 0.005. The blots are representative of three independent experiments. As the control of loading, the Ponceau Staining was shown. Then, HMEC-1 cells were cultured in medium supplemented with CM isolated from coculture of CAF-like cells and colon cancer or CAF-like cells maintained in colon cancer cell CM and treated, if necessary, with vincristine (+VIN) or NSAIDs (IBU or AsA). Then, elongation ratio ( n = 6) ( B ), capillary assay ( n = 9) ( C ), and level of contraction protein (caldesmon, tropomyosin), vimentin, and α-SMA were analyzed by Western blot ( D ), with GAPDH used as the loading control. The results are provided as means ± SD ( n = 3), ** p < 0.001, *** p < 0.005. The blots are representative of three independent experiments. The values from control cells are marked by dashed lines.

    Article Snippet: In particular experiments, the blots were incubated with primary antibodies recognizing α-SMA, tropomyosin, caldesmon, vimentin (cell signaling), TUBA, TUBB2, TUBB3, TUBB4, GAPDH and IL-6, TGF-β1 or TGF-β2.

    Techniques: Isolation, Western Blot, Staining, Cell Culture