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dlc1 sam  (Addgene inc)


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    Structured Review

    Addgene inc dlc1 sam
    The <t>SAM</t> domain of <t>DLC1</t> bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.
    Dlc1 Sam, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dlc1 sam/product/Addgene inc
    Average 91 stars, based on 2 article reviews
    dlc1 sam - by Bioz Stars, 2026-05
    91/100 stars

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    1) Product Images from "DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA"

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA119.011929

    The SAM domain of DLC1 bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.
    Figure Legend Snippet: The SAM domain of DLC1 bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.

    Techniques Used: Migration, Western Blot, Expressing, Mutagenesis, Immunoprecipitation

    The DLC1 SAM domain bound to peptides derived from PTEN or TNS3 C2 domain. A, peptide-walking arrays of the PTEN-C2 (aa 174–403) or TNS3-C2 domain (aa 166–440) were probed with purified GST-SAM and the bound protein detected by anti-GST Western blotting. Peptides representing phosphorylated peptides, which showed no binding, are identified in white boxes. See Fig. S1 for the peptide array map and peptide identities. B, sequence alignment of the PTEN and TNS3 C2 domains with the SAM-binding peptides/motifs identified in A are shown in black boxes. C, SAM-binding peptides from B mapped onto the structure of the PTEN-C2 domain (PDB code 1D5R, aa 188–351; 230GPTR peptide in green, 257FFHK in red, and 334NRYF in blue). D and E, binding of the SAM domain to peptides from PTEN (230GPTRREDKFMYF) or TNS3 (244CYHKKYRSATRD) C2 domains. Shown are representative binding curves from fluorescence polarization (FP) analysis (n = 3) using the corresponding fluorescein-labeled C2 peptides. ΔFP, difference in fluorescence polarization.
    Figure Legend Snippet: The DLC1 SAM domain bound to peptides derived from PTEN or TNS3 C2 domain. A, peptide-walking arrays of the PTEN-C2 (aa 174–403) or TNS3-C2 domain (aa 166–440) were probed with purified GST-SAM and the bound protein detected by anti-GST Western blotting. Peptides representing phosphorylated peptides, which showed no binding, are identified in white boxes. See Fig. S1 for the peptide array map and peptide identities. B, sequence alignment of the PTEN and TNS3 C2 domains with the SAM-binding peptides/motifs identified in A are shown in black boxes. C, SAM-binding peptides from B mapped onto the structure of the PTEN-C2 domain (PDB code 1D5R, aa 188–351; 230GPTR peptide in green, 257FFHK in red, and 334NRYF in blue). D and E, binding of the SAM domain to peptides from PTEN (230GPTRREDKFMYF) or TNS3 (244CYHKKYRSATRD) C2 domains. Shown are representative binding curves from fluorescence polarization (FP) analysis (n = 3) using the corresponding fluorescein-labeled C2 peptides. ΔFP, difference in fluorescence polarization.

    Techniques Used: Derivative Assay, Purification, Western Blot, Binding Assay, Peptide Microarray, Sequencing, Fluorescence, Labeling

    The C2 peptides disrupted the DLC1 SAM-PTEN/TNS3-C2 domain-domain interactions in cells. A and B, effect of the C2 peptides on DLC1-SAM binding to the TNS3-C2 domain in HEK293DLC1 cells without EGF stimulation. The TNS3 C2 domain bound more tightly to the DLC1 SAM domain in the absence of EGF stimulation; accordingly, the TNS3-C2–derived peptide inhibited this interaction more effectively than the PTEN C2–derived peptide. Quantification of the Western blots indicates a significantly different effect between the two C2 peptides at 5 μm (n = 3; *, p < 0.01, Student's t test). C and D, effect of the C2 peptides on DLC1-SAM binding to the PTEN C2 domain in HEK293 cells in the presence of EGF. The PTEN-C2 domain bound to the SAM domain more tightly with EGF stimulation (for 30 min). Accordingly, the PTEN C2–derived peptide blocked this interaction more effectively than the TNS3 C2–derived peptide in HEK293 cells with EGF. Quantification of Western blots (D) indicates a significantly different effect between the two C2 peptides at 5 μm peptide (n = 3; *, p < 0.01, Student's t test). Scr: scrambled TSN3-C2 peptide control, applied at 30 μm.
    Figure Legend Snippet: The C2 peptides disrupted the DLC1 SAM-PTEN/TNS3-C2 domain-domain interactions in cells. A and B, effect of the C2 peptides on DLC1-SAM binding to the TNS3-C2 domain in HEK293DLC1 cells without EGF stimulation. The TNS3 C2 domain bound more tightly to the DLC1 SAM domain in the absence of EGF stimulation; accordingly, the TNS3-C2–derived peptide inhibited this interaction more effectively than the PTEN C2–derived peptide. Quantification of the Western blots indicates a significantly different effect between the two C2 peptides at 5 μm (n = 3; *, p < 0.01, Student's t test). C and D, effect of the C2 peptides on DLC1-SAM binding to the PTEN C2 domain in HEK293 cells in the presence of EGF. The PTEN-C2 domain bound to the SAM domain more tightly with EGF stimulation (for 30 min). Accordingly, the PTEN C2–derived peptide blocked this interaction more effectively than the TNS3 C2–derived peptide in HEK293 cells with EGF. Quantification of Western blots (D) indicates a significantly different effect between the two C2 peptides at 5 μm peptide (n = 3; *, p < 0.01, Student's t test). Scr: scrambled TSN3-C2 peptide control, applied at 30 μm.

    Techniques Used: Binding Assay, Derivative Assay, Western Blot

    The C2 peptides decreased RhoA activity in multiple cell lines and reduced colony formation by DLC1-expressing HEK293 cells. A, both TNS3 and PTEN C2 peptides were able to inhibit RhoA activation in the DLC1-overexpressing HEK293DLC1 cells in a concentration-dependent manner. B and C, the same RhoA-GTP inhibitory effect was observed for the C2 peptides in EGF-treated MDA-MB-231 cells (B) or HGF-treated HCC78 cells (C). D, colony-formation in soft agar for the HEK293DLC1 cells in the absence (no treatment) or presence of a C2 peptide or the scrambled TNS3-C2 peptide. E, quantify of colony-formation data in D; *, denotes a p value < 0.01 (n = 3), Student's t test; IB, immunoblotting.
    Figure Legend Snippet: The C2 peptides decreased RhoA activity in multiple cell lines and reduced colony formation by DLC1-expressing HEK293 cells. A, both TNS3 and PTEN C2 peptides were able to inhibit RhoA activation in the DLC1-overexpressing HEK293DLC1 cells in a concentration-dependent manner. B and C, the same RhoA-GTP inhibitory effect was observed for the C2 peptides in EGF-treated MDA-MB-231 cells (B) or HGF-treated HCC78 cells (C). D, colony-formation in soft agar for the HEK293DLC1 cells in the absence (no treatment) or presence of a C2 peptide or the scrambled TNS3-C2 peptide. E, quantify of colony-formation data in D; *, denotes a p value < 0.01 (n = 3), Student's t test; IB, immunoblotting.

    Techniques Used: Activity Assay, Expressing, Activation Assay, Concentration Assay, Western Blot

    C2 peptides reduced anchorage-independent growth and EGF-dependent migration of breast cancer cells. A, colony formation by MDA-MB-231 cells treated with a C2 peptide or scrambled control (of tat-TNS3-C2) or transfected with DLC1-ΔSAM. B, quantification of data in A to show efficiency in colony formation for the above cells compared with the parent cells (set as 100%). C, representative images of wound-healing in peptide-treated MDA-MB-231 cells. D, quantification of the would-healing data in C. For panels B and D, * denotes p < 0.01 (compared with the scramble peptide, n = 3), Student's t test. E, Western blots of total and active RhoA in peptide-treated MDA-MB-231 cells in response to EGF treatment. Peptide concentration in C–E: 18 μm.
    Figure Legend Snippet: C2 peptides reduced anchorage-independent growth and EGF-dependent migration of breast cancer cells. A, colony formation by MDA-MB-231 cells treated with a C2 peptide or scrambled control (of tat-TNS3-C2) or transfected with DLC1-ΔSAM. B, quantification of data in A to show efficiency in colony formation for the above cells compared with the parent cells (set as 100%). C, representative images of wound-healing in peptide-treated MDA-MB-231 cells. D, quantification of the would-healing data in C. For panels B and D, * denotes p < 0.01 (compared with the scramble peptide, n = 3), Student's t test. E, Western blots of total and active RhoA in peptide-treated MDA-MB-231 cells in response to EGF treatment. Peptide concentration in C–E: 18 μm.

    Techniques Used: Migration, Transfection, Western Blot, Concentration Assay



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    dlc1 sam  (Addgene inc)
    91
    Addgene inc dlc1 sam
    The <t>SAM</t> domain of <t>DLC1</t> bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.
    Dlc1 Sam, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dlc1 sam/product/Addgene inc
    Average 91 stars, based on 1 article reviews
    dlc1 sam - by Bioz Stars, 2026-05
    91/100 stars
    		  Buy from Supplier

    Image Search Results


    The SAM domain of DLC1 bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.

    Journal: The Journal of Biological Chemistry

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    doi: 10.1074/jbc.RA119.011929

    Figure Lengend Snippet: The SAM domain of DLC1 bound to its own RhoGAP domain and the C2 domain of TNS3 or PTEN. A, a schematic depicting the interactions between the DLC1 SAM domain and the TNS3 or PTEN C2 domain and how these interactions regulate cell migration through the RhoGAP-RhoA pathway. B, Western blots (WB) confirming the SAM-C2 domain interaction in cells. HEK293 cells co-expressing GFP-fused PTEN-C2 (left panel) or TNS3-C2 (right panel) and FLAG-tagged full-length DLC1, DLC1-SAM (SAM domain only), or DLC1-ΔSAM (SAM deletion mutant) were subjected to immunoprecipitation (IP) and immunoblotting (IB) using anti-GFP and anti-FLAG antibodies.

    Article Snippet: DNA sequence encoding the DLC1-SAM (residues 13–78) was subcloned into the pGEX-2T vector (Addgene) for the expression of GST-SAM in Escherichia coli .

    Techniques: Migration, Western Blot, Expressing, Mutagenesis, Immunoprecipitation

    The DLC1 SAM domain bound to peptides derived from PTEN or TNS3 C2 domain. A, peptide-walking arrays of the PTEN-C2 (aa 174–403) or TNS3-C2 domain (aa 166–440) were probed with purified GST-SAM and the bound protein detected by anti-GST Western blotting. Peptides representing phosphorylated peptides, which showed no binding, are identified in white boxes. See Fig. S1 for the peptide array map and peptide identities. B, sequence alignment of the PTEN and TNS3 C2 domains with the SAM-binding peptides/motifs identified in A are shown in black boxes. C, SAM-binding peptides from B mapped onto the structure of the PTEN-C2 domain (PDB code 1D5R, aa 188–351; 230GPTR peptide in green, 257FFHK in red, and 334NRYF in blue). D and E, binding of the SAM domain to peptides from PTEN (230GPTRREDKFMYF) or TNS3 (244CYHKKYRSATRD) C2 domains. Shown are representative binding curves from fluorescence polarization (FP) analysis (n = 3) using the corresponding fluorescein-labeled C2 peptides. ΔFP, difference in fluorescence polarization.

    Journal: The Journal of Biological Chemistry

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    doi: 10.1074/jbc.RA119.011929

    Figure Lengend Snippet: The DLC1 SAM domain bound to peptides derived from PTEN or TNS3 C2 domain. A, peptide-walking arrays of the PTEN-C2 (aa 174–403) or TNS3-C2 domain (aa 166–440) were probed with purified GST-SAM and the bound protein detected by anti-GST Western blotting. Peptides representing phosphorylated peptides, which showed no binding, are identified in white boxes. See Fig. S1 for the peptide array map and peptide identities. B, sequence alignment of the PTEN and TNS3 C2 domains with the SAM-binding peptides/motifs identified in A are shown in black boxes. C, SAM-binding peptides from B mapped onto the structure of the PTEN-C2 domain (PDB code 1D5R, aa 188–351; 230GPTR peptide in green, 257FFHK in red, and 334NRYF in blue). D and E, binding of the SAM domain to peptides from PTEN (230GPTRREDKFMYF) or TNS3 (244CYHKKYRSATRD) C2 domains. Shown are representative binding curves from fluorescence polarization (FP) analysis (n = 3) using the corresponding fluorescein-labeled C2 peptides. ΔFP, difference in fluorescence polarization.

    Article Snippet: DNA sequence encoding the DLC1-SAM (residues 13–78) was subcloned into the pGEX-2T vector (Addgene) for the expression of GST-SAM in Escherichia coli .

    Techniques: Derivative Assay, Purification, Western Blot, Binding Assay, Peptide Microarray, Sequencing, Fluorescence, Labeling

    The C2 peptides disrupted the DLC1 SAM-PTEN/TNS3-C2 domain-domain interactions in cells. A and B, effect of the C2 peptides on DLC1-SAM binding to the TNS3-C2 domain in HEK293DLC1 cells without EGF stimulation. The TNS3 C2 domain bound more tightly to the DLC1 SAM domain in the absence of EGF stimulation; accordingly, the TNS3-C2–derived peptide inhibited this interaction more effectively than the PTEN C2–derived peptide. Quantification of the Western blots indicates a significantly different effect between the two C2 peptides at 5 μm (n = 3; *, p < 0.01, Student's t test). C and D, effect of the C2 peptides on DLC1-SAM binding to the PTEN C2 domain in HEK293 cells in the presence of EGF. The PTEN-C2 domain bound to the SAM domain more tightly with EGF stimulation (for 30 min). Accordingly, the PTEN C2–derived peptide blocked this interaction more effectively than the TNS3 C2–derived peptide in HEK293 cells with EGF. Quantification of Western blots (D) indicates a significantly different effect between the two C2 peptides at 5 μm peptide (n = 3; *, p < 0.01, Student's t test). Scr: scrambled TSN3-C2 peptide control, applied at 30 μm.

    Journal: The Journal of Biological Chemistry

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    doi: 10.1074/jbc.RA119.011929

    Figure Lengend Snippet: The C2 peptides disrupted the DLC1 SAM-PTEN/TNS3-C2 domain-domain interactions in cells. A and B, effect of the C2 peptides on DLC1-SAM binding to the TNS3-C2 domain in HEK293DLC1 cells without EGF stimulation. The TNS3 C2 domain bound more tightly to the DLC1 SAM domain in the absence of EGF stimulation; accordingly, the TNS3-C2–derived peptide inhibited this interaction more effectively than the PTEN C2–derived peptide. Quantification of the Western blots indicates a significantly different effect between the two C2 peptides at 5 μm (n = 3; *, p < 0.01, Student's t test). C and D, effect of the C2 peptides on DLC1-SAM binding to the PTEN C2 domain in HEK293 cells in the presence of EGF. The PTEN-C2 domain bound to the SAM domain more tightly with EGF stimulation (for 30 min). Accordingly, the PTEN C2–derived peptide blocked this interaction more effectively than the TNS3 C2–derived peptide in HEK293 cells with EGF. Quantification of Western blots (D) indicates a significantly different effect between the two C2 peptides at 5 μm peptide (n = 3; *, p < 0.01, Student's t test). Scr: scrambled TSN3-C2 peptide control, applied at 30 μm.

    Article Snippet: DNA sequence encoding the DLC1-SAM (residues 13–78) was subcloned into the pGEX-2T vector (Addgene) for the expression of GST-SAM in Escherichia coli .

    Techniques: Binding Assay, Derivative Assay, Western Blot

    The C2 peptides decreased RhoA activity in multiple cell lines and reduced colony formation by DLC1-expressing HEK293 cells. A, both TNS3 and PTEN C2 peptides were able to inhibit RhoA activation in the DLC1-overexpressing HEK293DLC1 cells in a concentration-dependent manner. B and C, the same RhoA-GTP inhibitory effect was observed for the C2 peptides in EGF-treated MDA-MB-231 cells (B) or HGF-treated HCC78 cells (C). D, colony-formation in soft agar for the HEK293DLC1 cells in the absence (no treatment) or presence of a C2 peptide or the scrambled TNS3-C2 peptide. E, quantify of colony-formation data in D; *, denotes a p value < 0.01 (n = 3), Student's t test; IB, immunoblotting.

    Journal: The Journal of Biological Chemistry

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    doi: 10.1074/jbc.RA119.011929

    Figure Lengend Snippet: The C2 peptides decreased RhoA activity in multiple cell lines and reduced colony formation by DLC1-expressing HEK293 cells. A, both TNS3 and PTEN C2 peptides were able to inhibit RhoA activation in the DLC1-overexpressing HEK293DLC1 cells in a concentration-dependent manner. B and C, the same RhoA-GTP inhibitory effect was observed for the C2 peptides in EGF-treated MDA-MB-231 cells (B) or HGF-treated HCC78 cells (C). D, colony-formation in soft agar for the HEK293DLC1 cells in the absence (no treatment) or presence of a C2 peptide or the scrambled TNS3-C2 peptide. E, quantify of colony-formation data in D; *, denotes a p value < 0.01 (n = 3), Student's t test; IB, immunoblotting.

    Article Snippet: DNA sequence encoding the DLC1-SAM (residues 13–78) was subcloned into the pGEX-2T vector (Addgene) for the expression of GST-SAM in Escherichia coli .

    Techniques: Activity Assay, Expressing, Activation Assay, Concentration Assay, Western Blot

    C2 peptides reduced anchorage-independent growth and EGF-dependent migration of breast cancer cells. A, colony formation by MDA-MB-231 cells treated with a C2 peptide or scrambled control (of tat-TNS3-C2) or transfected with DLC1-ΔSAM. B, quantification of data in A to show efficiency in colony formation for the above cells compared with the parent cells (set as 100%). C, representative images of wound-healing in peptide-treated MDA-MB-231 cells. D, quantification of the would-healing data in C. For panels B and D, * denotes p < 0.01 (compared with the scramble peptide, n = 3), Student's t test. E, Western blots of total and active RhoA in peptide-treated MDA-MB-231 cells in response to EGF treatment. Peptide concentration in C–E: 18 μm.

    Journal: The Journal of Biological Chemistry

    Article Title: DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA

    doi: 10.1074/jbc.RA119.011929

    Figure Lengend Snippet: C2 peptides reduced anchorage-independent growth and EGF-dependent migration of breast cancer cells. A, colony formation by MDA-MB-231 cells treated with a C2 peptide or scrambled control (of tat-TNS3-C2) or transfected with DLC1-ΔSAM. B, quantification of data in A to show efficiency in colony formation for the above cells compared with the parent cells (set as 100%). C, representative images of wound-healing in peptide-treated MDA-MB-231 cells. D, quantification of the would-healing data in C. For panels B and D, * denotes p < 0.01 (compared with the scramble peptide, n = 3), Student's t test. E, Western blots of total and active RhoA in peptide-treated MDA-MB-231 cells in response to EGF treatment. Peptide concentration in C–E: 18 μm.

    Article Snippet: DNA sequence encoding the DLC1-SAM (residues 13–78) was subcloned into the pGEX-2T vector (Addgene) for the expression of GST-SAM in Escherichia coli .

    Techniques: Migration, Transfection, Western Blot, Concentration Assay