anti hdac1 (Danaher Inc)

Danaher Inc anti hdac1

APPL1 is a part of the <t>β-catenin-Reptin-HDAC1/2</t> complex. A , HEK293 cell lysates were subjected to a coimmunoprecipitation assay ( IP ) using anti-Reptin or control IgG, and the resultant precipitates were subjected to immunoblotting ( IB ) with the indicated antibodies. TCL , total cell lysate. B , a 2D BN/SDS-PAGE analysis of HEK293 cell extracts. Multiprotein complexes were resolved on 6–13% acrylamide gradient gel, followed by Tris-glycine-SDS-PAGE (8% gel). Immunoblotting was performed with specific antibodies recognizing the indicated proteins.

Anti Hdac1, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab198495/Recombinant+Dengue+virus+2+Dengue+Virus+NS1+glycoprotein/pmc02709337-16-10-23
Average 99 stars, based on 1 article reviews

anti hdac1 - by Bioz Stars, 2026-10

99/100 stars

Buy from Supplier

anti oct 3 4 (Danaher Inc)

Danaher Inc anti oct 3 4

Anti Oct 3 4, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab198495/Recombinant+rat+GM-CSF+protein/pm29620155-73-8-12
Average 99 stars, based on 1 article reviews

anti oct 3 4 - by Bioz Stars, 2026-10

99/100 stars

Buy from Supplier

mouse antihuman cd86 primary antibodies (Danaher Inc)

Danaher Inc mouse antihuman cd86 primary antibodies

M1‐ and M2‐polarized macrophages in BC tissues with different expression of FREM1. (A) BC tissues were first divided into low‐ and high‐FREM1 group as described previously. IF was conducted to assess the presence of <t>CD86</t> + CD163 − M1‐polarized and CD86 − CD163 + M2‐polarized macrophages in low‐ and high‐FREM1 group. Simples were double stained for CD86‐Alexa Fluor‐647 (red) and CD163‐Alexa Fluor‐488 (green). DAPI represents nuclei of the cells (blue). Images are shown individually and as an overlay of the fluorescence channels on the far right. Scatter plots displaying the quantitative data of (B) CD86 + and (C) CD163 + cells in FREM‐low and FREM1‐high group. Solid lines in the scatter plots delineate the mean ± SD. * p < 0.05, *** p < 0.001

Mouse Antihuman Cd86 Primary Antibodies, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab198495/Abcam+Phospate+Buffered+Saline%2C+1+Pack/pmc07774739-98-5-10
Average 99 stars, based on 1 article reviews

mouse antihuman cd86 primary antibodies - by Bioz Stars, 2026-10

99/100 stars

Buy from Supplier

phosphodna pk s2056 (Danaher Inc)

Danaher Inc phosphodna pk s2056

Phosphodna Pk S2056, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab198495/Recombinant+Dengue+virus+1+NS1+protein/pm30725116-56-23-24
Average 99 stars, based on 1 article reviews

phosphodna pk s2056 - by Bioz Stars, 2026-10

99/100 stars

Buy from Supplier

Image Search Results

APPL1 is a part of the β-catenin-Reptin-HDAC1/2 complex. A , HEK293 cell lysates were subjected to a coimmunoprecipitation assay ( IP ) using anti-Reptin or control IgG, and the resultant precipitates were subjected to immunoblotting ( IB ) with the indicated antibodies. TCL , total cell lysate. B , a 2D BN/SDS-PAGE analysis of HEK293 cell extracts. Multiprotein complexes were resolved on 6–13% acrylamide gradient gel, followed by Tris-glycine-SDS-PAGE (8% gel). Immunoblotting was performed with specific antibodies recognizing the indicated proteins.

Journal:

Article Title:

doi:

Figure Lengend Snippet: APPL1 is a part of the β-catenin-Reptin-HDAC1/2 complex. A , HEK293 cell lysates were subjected to a coimmunoprecipitation assay ( IP ) using anti-Reptin or control IgG, and the resultant precipitates were subjected to immunoblotting ( IB ) with the indicated antibodies. TCL , total cell lysate. B , a 2D BN/SDS-PAGE analysis of HEK293 cell extracts. Multiprotein complexes were resolved on 6–13% acrylamide gradient gel, followed by Tris-glycine-SDS-PAGE (8% gel). Immunoblotting was performed with specific antibodies recognizing the indicated proteins.

Article Snippet: The following antibodies were used: anti-Reptin (catalog number ab36569; Abcam), anti-HDAC1 (for immunoblotting (catalog number ab19845) and for chromatin immunoprecipitation (catalog number ab46985); Abcam), anti-Myc (catalog number 05-419; 9E10; Upstate Biotechnology, Inc.), anti-β-catenin (catalog number 610154; BD Bioscience), anti-HA (catalog number sc-805; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), anti-GAPDH (catalog number sc-25778; Santa Cruz Biotechnology), anti-His (catalog number 34660; Qiagen), anti-GST (catalog number 27-4577; GE Healthcare), and anti-HDAC2 (catalog number 05-814; Upstate Biotechnology).

Techniques: Co-Immunoprecipitation Assay, Western Blot, SDS Page

Overexpression of APPL proteins reduces the amounts of HDACs bound to Reptin. A , HEK293 cells were transiently transfected with APPL1-Myc and APPL2-Myc. Forty-eight hours post-transfection, cell extracts were prepared, and a coimmunoprecipitation assay ( IP ) was performed with either anti-Reptin or control IgG. The resultant precipitates were analyzed by immunoblotting ( IB ) against the indicated antibodies ( A ) or were subjected to fluorometric assays for measuring the respective HDAC activities ( C ). Each HDAC activity assay was performed in duplicate, and relative fluorescence unit ( RFU ) values shown are the averages ± S.D. from which the RFU values of assay buffer were subtracted. B , HEK293 cells were cotransfected with plasmids encoding YFP-tagged APPL1 or empty vector. Cell extracts were prepared and immunoprecipitated using anti-HDAC2. Bound proteins were separated and visualized by immunoblotting using anti-HDAC2, anti-HDAC1, anti-Reptin, and anti-APPL1 antibodies.

Journal:

Article Title:

doi:

Figure Lengend Snippet: Overexpression of APPL proteins reduces the amounts of HDACs bound to Reptin. A , HEK293 cells were transiently transfected with APPL1-Myc and APPL2-Myc. Forty-eight hours post-transfection, cell extracts were prepared, and a coimmunoprecipitation assay ( IP ) was performed with either anti-Reptin or control IgG. The resultant precipitates were analyzed by immunoblotting ( IB ) against the indicated antibodies ( A ) or were subjected to fluorometric assays for measuring the respective HDAC activities ( C ). Each HDAC activity assay was performed in duplicate, and relative fluorescence unit ( RFU ) values shown are the averages ± S.D. from which the RFU values of assay buffer were subtracted. B , HEK293 cells were cotransfected with plasmids encoding YFP-tagged APPL1 or empty vector. Cell extracts were prepared and immunoprecipitated using anti-HDAC2. Bound proteins were separated and visualized by immunoblotting using anti-HDAC2, anti-HDAC1, anti-Reptin, and anti-APPL1 antibodies.

Techniques: Over Expression, Transfection, Co-Immunoprecipitation Assay, Western Blot, HDAC Activity Assay, Fluorescence, Plasmid Preparation, Immunoprecipitation

Recruitment of β-catenin, Reptin, and HDAC1 to the promoters of Wnt target genes is affected upon overexpression of APPL proteins. A , overexpression of APPL proteins reduces the amount of Reptin bound to β-catenin. HEK293 cells were transiently transfected with APPL1 or APPL2. Thirty-six hours post-transfection, cells were treated with Wnt3a-conditioned medium for 4 h. Subsequently, cell extracts were prepared, and a coimmunoprecipitation assay ( IP ) was performed with anti-β-catenin or control IgG. The resulting precipitates were analyzed by immunoblotting ( IB ) with the indicated antibodies. B , APPL proteins increase the recruitment of β-catenin and reduce the amounts of Reptin and HDAC1 at the Wnt target gene promoters. HEK293 cells were transfected with either empty pcDNA 3.1 ( lane 1 ) or plasmids expressing APPL1 ( lane 2 ) and APPL2 ( lane 3 ). Thirty-six hours post-transfection, cells were treated with Wnt3a-conditioned medium for 4 h and then subjected to chromatin immunoprecipitation using anti-β-catenin, anti-HDAC1, and anti-Reptin antibodies. PCR was performed from these immunoprecipitates by using the primer pair covering the β-catenin binding sites at the promoters of cyclin D1 and Axin2. PCR products were resolved by agarose gel and stained with ethidium bromide. Lane c , PCR mixture without template.

Journal:

Article Title:

doi:

Figure Lengend Snippet: Recruitment of β-catenin, Reptin, and HDAC1 to the promoters of Wnt target genes is affected upon overexpression of APPL proteins. A , overexpression of APPL proteins reduces the amount of Reptin bound to β-catenin. HEK293 cells were transiently transfected with APPL1 or APPL2. Thirty-six hours post-transfection, cells were treated with Wnt3a-conditioned medium for 4 h. Subsequently, cell extracts were prepared, and a coimmunoprecipitation assay ( IP ) was performed with anti-β-catenin or control IgG. The resulting precipitates were analyzed by immunoblotting ( IB ) with the indicated antibodies. B , APPL proteins increase the recruitment of β-catenin and reduce the amounts of Reptin and HDAC1 at the Wnt target gene promoters. HEK293 cells were transfected with either empty pcDNA 3.1 ( lane 1 ) or plasmids expressing APPL1 ( lane 2 ) and APPL2 ( lane 3 ). Thirty-six hours post-transfection, cells were treated with Wnt3a-conditioned medium for 4 h and then subjected to chromatin immunoprecipitation using anti-β-catenin, anti-HDAC1, and anti-Reptin antibodies. PCR was performed from these immunoprecipitates by using the primer pair covering the β-catenin binding sites at the promoters of cyclin D1 and Axin2. PCR products were resolved by agarose gel and stained with ethidium bromide. Lane c , PCR mixture without template.

Techniques: Over Expression, Transfection, Co-Immunoprecipitation Assay, Western Blot, Expressing, Chromatin Immunoprecipitation, Binding Assay, Agarose Gel Electrophoresis, Staining

Journal: Cancer Medicine

Article Title: Elevated expression of FREM1 in breast cancer indicates favorable prognosis and high‐level immune infiltration status

doi: 10.1002/cam4.3543

Figure Lengend Snippet: M1‐ and M2‐polarized macrophages in BC tissues with different expression of FREM1. (A) BC tissues were first divided into low‐ and high‐FREM1 group as described previously. IF was conducted to assess the presence of CD86 + CD163 − M1‐polarized and CD86 − CD163 + M2‐polarized macrophages in low‐ and high‐FREM1 group. Simples were double stained for CD86‐Alexa Fluor‐647 (red) and CD163‐Alexa Fluor‐488 (green). DAPI represents nuclei of the cells (blue). Images are shown individually and as an overlay of the fluorescence channels on the far right. Scatter plots displaying the quantitative data of (B) CD86 + and (C) CD163 + cells in FREM‐low and FREM1‐high group. Solid lines in the scatter plots delineate the mean ± SD. * p < 0.05, *** p < 0.001

Article Snippet: Slides were then incubated with mouse antihuman CD86 primary antibodies (Abcam, ab270719, 2 µg/ml) for 2 h at room temperature.

Techniques: Expressing, Staining, Fluorescence

ab198495 Search Results

Image Search Results