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anti fam98a  (Bioss)


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    Structured Review

    Bioss anti fam98a
    Identification of the sequence within <t>FAM98A</t> required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).
    Anti Fam98a, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti fam98a/product/Bioss
    Average 94 stars, based on 4 article reviews
    anti fam98a - by Bioz Stars, 2026-02
    94/100 stars

    Images

    1) Product Images from "Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway"

    Article Title: Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkaf150

    Identification of the sequence within FAM98A required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).
    Figure Legend Snippet: Identification of the sequence within FAM98A required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).

    Techniques Used: Sequencing, Binding Assay, Incubation, Staining, Western Blot, Immunoprecipitation, Comparison, Far Western Blot, Mutagenesis

    Interaction between DNA-PKcs and ARID1A facilitates late-stage NHEJ processes. ( A and B ) HCT116 WT and F3640A mutant cells were transfected with GFP-fused plasmids, GFP-KU80 and GFP-LIG4, for 24 h before irradiation. Following laser microirradiation, live-cell imaging was performed, capturing images every 10 s for 200 s. Representative images (upper panel) and quantification of signal intensity over 200 s (lower panel) of GFP-KU80 (A) and GFP-LIG4 (B) at DSB sites are shown. Scale bar: 10 μm. Statistical significance (Mann–Whitney U-test): ns, nonsignificant; *** P < 0.001. ( C ) ARM domain of ARID1A interacts with FAM98A and DNA-PKcs via their novel binding sites. ( D ) Proposed model of ARID1A in DSB repair. The DNA-PKcs–ARID1A interaction facilitates late-stage NHEJ processes, including PQR autophosphorylation and LIG4 recruitment, following KU70/80 and DNA-PKcs recruitment and activation at DSB sites. Through its interaction with DNA-PKcs, ARID1A, as part of the SWI/SNF complex, may promote nucleosome remodeling around DSB sites to support NHEJ. This interaction is proposed to induce conformational changes between DNA ends and the DNA-PKcs/KU70/80 complex, altering the autophosphorylation status of DNA-PKcs and enabling the recruitment of additional NHEJ factors, such as LIG4, during late-stage NHEJ.
    Figure Legend Snippet: Interaction between DNA-PKcs and ARID1A facilitates late-stage NHEJ processes. ( A and B ) HCT116 WT and F3640A mutant cells were transfected with GFP-fused plasmids, GFP-KU80 and GFP-LIG4, for 24 h before irradiation. Following laser microirradiation, live-cell imaging was performed, capturing images every 10 s for 200 s. Representative images (upper panel) and quantification of signal intensity over 200 s (lower panel) of GFP-KU80 (A) and GFP-LIG4 (B) at DSB sites are shown. Scale bar: 10 μm. Statistical significance (Mann–Whitney U-test): ns, nonsignificant; *** P < 0.001. ( C ) ARM domain of ARID1A interacts with FAM98A and DNA-PKcs via their novel binding sites. ( D ) Proposed model of ARID1A in DSB repair. The DNA-PKcs–ARID1A interaction facilitates late-stage NHEJ processes, including PQR autophosphorylation and LIG4 recruitment, following KU70/80 and DNA-PKcs recruitment and activation at DSB sites. Through its interaction with DNA-PKcs, ARID1A, as part of the SWI/SNF complex, may promote nucleosome remodeling around DSB sites to support NHEJ. This interaction is proposed to induce conformational changes between DNA ends and the DNA-PKcs/KU70/80 complex, altering the autophosphorylation status of DNA-PKcs and enabling the recruitment of additional NHEJ factors, such as LIG4, during late-stage NHEJ.

    Techniques Used: Mutagenesis, Transfection, Irradiation, Live Cell Imaging, MANN-WHITNEY, Binding Assay, Activation Assay



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    anti fam98a  (Bioss)
    94
    Bioss anti fam98a
    Identification of the sequence within <t>FAM98A</t> required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).
    Anti Fam98a, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti fam98a/product/Bioss
    Average 94 stars, based on 1 article reviews
    anti fam98a - by Bioz Stars, 2026-02
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    Identification of the sequence within FAM98A required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).

    Journal: Nucleic Acids Research

    Article Title: Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway

    doi: 10.1093/nar/gkaf150

    Figure Lengend Snippet: Identification of the sequence within FAM98A required for binding with ARID1A. ( A ) GST-fusion proteins with ARID1A mutants: (i) GST–ARID1A–N-terminal region (1–980 aa), (ii) GST–ARID1A–ARID domain (981–1140 aa), (iii) GST–ARID1A–HIC domain (1141–1641 aa), (iv) GST–ARID1A–C-terminal region (1634–1913 aa), (v) GST–ARID1A–ARM domain (1914–2285 aa). ARID: AT-rich interaction domain (1000–1120 aa), HIC1: hypermethylated in cancer 1 binding domain (1355–1451 aa), ARM: Armadillo domain (1974–2231 aa), and LXXLL: Leu-X-X-Leu-Leu sequence, a protein-recognition motif widely used in transcriptional regulation. ( B ) Mapping of the ARID1A region required for binding with interacting proteins; HEK293 nuclear extract was incubated with GST–ARID1A mutants, and interacting proteins were detected using the indicated antibodies. In addition, protein staining of GST–ARID1A mutants is shown (lower panel). IB, immunoblot. ( C ) FAM98A interacts with ARID1A and ARID1B. Endogenous ARID1A or ARID1B was immunoprecipitated with anti-ARID1A or -ARID1B, and FAM98A was probed by immunoblotting. ( D ) FAM98A interacts with ARID1A and ARID1B through their ARM domain. The nuclear extract was incubated with GST–ARID1A–ARM or ARID1B–ARM, and FAM98A was detected by immunoblot analysis. GST–ARID1B–ARM: ARM domain of ARID1B (aa 1861–2236). ( E ) Mass analysis data of FAM98A and FAM98B. ( F ) Comparison of the structures of FAM98A and FAM98B. FAM98A possesses a unique sequence in its C-terminal region. A sequence containing two adjacent phenylalanine residues is indicated. CH: calponin homology-like domain, black: highly conserved regions between FAM98A and FAM98B, dark gray: sequence-specific to FAM98A, and light gray: sequence-specific to FAM98B. ( G ) (Upper panel) Far-western blotting was used to detect the binding capacity of the wild-type, F495A mutant, or F499A mutant of the GST-fused C-terminal region of FAM98A (aa 479–519) to the His-tagged ARM domain of ARID1A. Protein staining of the GST-FAM98A C-terminal region is also shown (bottom panel).

    Article Snippet: Cells were incubated with anti-phospho-H2AX (05-636, Millipore), anti-53BP1 (A300-272A, Betyl), anti-FAM98A (Bioss Antibodies BS-11012R), anti-ARID1A (Sigma, HPA005456), and DNA-PKcs (G-4, sc-5282, Santa Cruz) antibodies for 1 h, washed three times with PBS-T, and incubated with Alexa Fluor 488 and Alexa Fluor 564 secondary antibody (Thermo Fisher) and 1 μM 4',6-diamidino-2-phenylindole (DAPI) for 1 h. Cells were washed three times with PBS-T and mounted in 1,4-diazabicyclo[2.2.2]octane (DABCO).

    Techniques: Sequencing, Binding Assay, Incubation, Staining, Western Blot, Immunoprecipitation, Comparison, Far Western Blot, Mutagenesis

    Interaction between DNA-PKcs and ARID1A facilitates late-stage NHEJ processes. ( A and B ) HCT116 WT and F3640A mutant cells were transfected with GFP-fused plasmids, GFP-KU80 and GFP-LIG4, for 24 h before irradiation. Following laser microirradiation, live-cell imaging was performed, capturing images every 10 s for 200 s. Representative images (upper panel) and quantification of signal intensity over 200 s (lower panel) of GFP-KU80 (A) and GFP-LIG4 (B) at DSB sites are shown. Scale bar: 10 μm. Statistical significance (Mann–Whitney U-test): ns, nonsignificant; *** P < 0.001. ( C ) ARM domain of ARID1A interacts with FAM98A and DNA-PKcs via their novel binding sites. ( D ) Proposed model of ARID1A in DSB repair. The DNA-PKcs–ARID1A interaction facilitates late-stage NHEJ processes, including PQR autophosphorylation and LIG4 recruitment, following KU70/80 and DNA-PKcs recruitment and activation at DSB sites. Through its interaction with DNA-PKcs, ARID1A, as part of the SWI/SNF complex, may promote nucleosome remodeling around DSB sites to support NHEJ. This interaction is proposed to induce conformational changes between DNA ends and the DNA-PKcs/KU70/80 complex, altering the autophosphorylation status of DNA-PKcs and enabling the recruitment of additional NHEJ factors, such as LIG4, during late-stage NHEJ.

    Journal: Nucleic Acids Research

    Article Title: Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway

    doi: 10.1093/nar/gkaf150

    Figure Lengend Snippet: Interaction between DNA-PKcs and ARID1A facilitates late-stage NHEJ processes. ( A and B ) HCT116 WT and F3640A mutant cells were transfected with GFP-fused plasmids, GFP-KU80 and GFP-LIG4, for 24 h before irradiation. Following laser microirradiation, live-cell imaging was performed, capturing images every 10 s for 200 s. Representative images (upper panel) and quantification of signal intensity over 200 s (lower panel) of GFP-KU80 (A) and GFP-LIG4 (B) at DSB sites are shown. Scale bar: 10 μm. Statistical significance (Mann–Whitney U-test): ns, nonsignificant; *** P < 0.001. ( C ) ARM domain of ARID1A interacts with FAM98A and DNA-PKcs via their novel binding sites. ( D ) Proposed model of ARID1A in DSB repair. The DNA-PKcs–ARID1A interaction facilitates late-stage NHEJ processes, including PQR autophosphorylation and LIG4 recruitment, following KU70/80 and DNA-PKcs recruitment and activation at DSB sites. Through its interaction with DNA-PKcs, ARID1A, as part of the SWI/SNF complex, may promote nucleosome remodeling around DSB sites to support NHEJ. This interaction is proposed to induce conformational changes between DNA ends and the DNA-PKcs/KU70/80 complex, altering the autophosphorylation status of DNA-PKcs and enabling the recruitment of additional NHEJ factors, such as LIG4, during late-stage NHEJ.

    Article Snippet: Cells were incubated with anti-phospho-H2AX (05-636, Millipore), anti-53BP1 (A300-272A, Betyl), anti-FAM98A (Bioss Antibodies BS-11012R), anti-ARID1A (Sigma, HPA005456), and DNA-PKcs (G-4, sc-5282, Santa Cruz) antibodies for 1 h, washed three times with PBS-T, and incubated with Alexa Fluor 488 and Alexa Fluor 564 secondary antibody (Thermo Fisher) and 1 μM 4',6-diamidino-2-phenylindole (DAPI) for 1 h. Cells were washed three times with PBS-T and mounted in 1,4-diazabicyclo[2.2.2]octane (DABCO).

    Techniques: Mutagenesis, Transfection, Irradiation, Live Cell Imaging, MANN-WHITNEY, Binding Assay, Activation Assay