polyclonal rabbit antibodies Search Results


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  • 99
    Millipore polyclonal rabbit antibodies
    Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in the cerebellar cortex of 10-d-old rats. Immunohistochemical labeling was performed on 10-μm-thick frontal rat cerebellar sections showing the EGL, the ML, the PCL, and the IGL. The labeling with <t>polyclonal</t> antibodies was enhanced using the fluorescein tyramide signal amplification system (New England Nuclear). In the EGL, MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and to less extents for TIMP 3 ( F ), were seen in granular precursor cells. In addition, MMP 9 was detected along the Bergmann glial fibers in this layer ( C ). Arrows point to strips of stained granular precursor cells. In the ML, MMP 3, MMP 9, and TIMP 1 were diffusely present over PK cells dendrites, whereas TIMP 3 was restricted to the cytoplasm of the PK cell dendrites (the small arrow in F points to the labeled PK cell dendritic arborization). In the PCL, the PK cell somata showed labeling for each marker, and MMP 9 expression was seen in the Bergmann glial cell somata. Some granular cells in the IGL were immunopositive for MMPs 3 and 9 and TIMPs 1, 2, and 3. Scale bar, 50 μm.
    Polyclonal Rabbit Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 308 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies rabbit polyclonal ab
    Anti-hsp90 antibodies increase NadA Δ351–405 monocyte stimulation in a polymixin B insensitive-way. A) Cells were treated with NadA Δ351–405 in the absence (black circles) or in the presence (open circles) of purified rabbit <t>polyclonal</t> antibodies directed to the COOH terminal domain of hsp90. Open squares refers to cells incubated with NadA Δ351–405 in the presence of purified rabbit polyclonal antibodies from non immunized animals. The indicated cytokines/chemokines were analyzed in the extracellular medium by BioPlex suspension arrays. Data are the mean from a representative experiment out of four run in triplicate. Bars are +/− SE. Asterisk indicates signals significantly different (p
    Rabbit Polyclonal Ab, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam rabbit polyclonal ab
    CDX2 immunolabelling controls. The binding specificity of the rabbit <t>polyclonal</t> anti CDX2 primary antibody (ab88129) (a) and mouse monoclonal anti CDX2 primary antibody (ab15258) (b) was verified with the use of blocking peptide (ab99158) prior to the antibody staining. The secondary antibodies used were goat anti-rabbit Rhodamine conjugated (sc-2091) in (a) and goat anti-mouse Rhodamine conjugated (sc-2092) in (b) . Dashed circle marks the metaphase plate. DAPI labels chromatin.
    Rabbit Polyclonal Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 719 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit polyclonal abs
    CDX2 immunolabelling controls. The binding specificity of the rabbit <t>polyclonal</t> anti CDX2 primary antibody (ab88129) (a) and mouse monoclonal anti CDX2 primary antibody (ab15258) (b) was verified with the use of blocking peptide (ab99158) prior to the antibody staining. The secondary antibodies used were goat anti-rabbit Rhodamine conjugated (sc-2091) in (a) and goat anti-mouse Rhodamine conjugated (sc-2092) in (b) . Dashed circle marks the metaphase plate. DAPI labels chromatin.
    Rabbit Polyclonal Abs, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bethyl rabbit polyclonal ab
    CDX2 immunolabelling controls. The binding specificity of the rabbit <t>polyclonal</t> anti CDX2 primary antibody (ab88129) (a) and mouse monoclonal anti CDX2 primary antibody (ab15258) (b) was verified with the use of blocking peptide (ab99158) prior to the antibody staining. The secondary antibodies used were goat anti-rabbit Rhodamine conjugated (sc-2091) in (a) and goat anti-mouse Rhodamine conjugated (sc-2092) in (b) . Dashed circle marks the metaphase plate. DAPI labels chromatin.
    Rabbit Polyclonal Ab, supplied by Bethyl, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology rabbit polyclonal ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Ab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 297 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Hypoxyprobe rabbit polyclonal ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Ab, supplied by Hypoxyprobe, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare rabbit polyclonal ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Ab, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Abcam rabbit polyclonal egfp antibody ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Egfp Antibody Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit polyclonal ab 4447
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Ab 4447, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies rabbit polyclonal antifibrinogen ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Antifibrinogen Ab, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal errγ ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Errγ Ab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Abcam polyclonal rabbit anti gprin1 antibody ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Polyclonal Rabbit Anti Gprin1 Antibody Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rabbit polyclonal aβ ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Aβ Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Synaptic Systems rabbit polyclonal snap23 ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Snap23 Ab, supplied by Synaptic Systems, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Proteintech rabbit stub1 polyclonal
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Stub1 Polyclonal, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Boster Bio rabbit polyclonal tlr4 ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Tlr4 Ab, supplied by Boster Bio, used in various techniques. Bioz Stars score: 89/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rabbit polyclonal antinitrotyrosine ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Antinitrotyrosine Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit polyclonal ab 12277
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Rabbit Polyclonal Ab 12277, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene gas1 rabbit polyclonal ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Gas1 Rabbit Polyclonal Ab, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Abcam foxp3 rabbit polyclonal ab
    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit <t>polyclonal</t> Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.
    Foxp3 Rabbit Polyclonal Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in the cerebellar cortex of 10-d-old rats. Immunohistochemical labeling was performed on 10-μm-thick frontal rat cerebellar sections showing the EGL, the ML, the PCL, and the IGL. The labeling with polyclonal antibodies was enhanced using the fluorescein tyramide signal amplification system (New England Nuclear). In the EGL, MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and to less extents for TIMP 3 ( F ), were seen in granular precursor cells. In addition, MMP 9 was detected along the Bergmann glial fibers in this layer ( C ). Arrows point to strips of stained granular precursor cells. In the ML, MMP 3, MMP 9, and TIMP 1 were diffusely present over PK cells dendrites, whereas TIMP 3 was restricted to the cytoplasm of the PK cell dendrites (the small arrow in F points to the labeled PK cell dendritic arborization). In the PCL, the PK cell somata showed labeling for each marker, and MMP 9 expression was seen in the Bergmann glial cell somata. Some granular cells in the IGL were immunopositive for MMPs 3 and 9 and TIMPs 1, 2, and 3. Scale bar, 50 μm.

    Journal: The Journal of Neuroscience

    Article Title: Spatiotemporal Expression Patterns of Metalloproteinases and Their Inhibitors in the Postnatal Developing Rat Cerebellum

    doi: 10.1523/JNEUROSCI.19-12-04994.1999

    Figure Lengend Snippet: Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in the cerebellar cortex of 10-d-old rats. Immunohistochemical labeling was performed on 10-μm-thick frontal rat cerebellar sections showing the EGL, the ML, the PCL, and the IGL. The labeling with polyclonal antibodies was enhanced using the fluorescein tyramide signal amplification system (New England Nuclear). In the EGL, MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and to less extents for TIMP 3 ( F ), were seen in granular precursor cells. In addition, MMP 9 was detected along the Bergmann glial fibers in this layer ( C ). Arrows point to strips of stained granular precursor cells. In the ML, MMP 3, MMP 9, and TIMP 1 were diffusely present over PK cells dendrites, whereas TIMP 3 was restricted to the cytoplasm of the PK cell dendrites (the small arrow in F points to the labeled PK cell dendritic arborization). In the PCL, the PK cell somata showed labeling for each marker, and MMP 9 expression was seen in the Bergmann glial cell somata. Some granular cells in the IGL were immunopositive for MMPs 3 and 9 and TIMPs 1, 2, and 3. Scale bar, 50 μm.

    Article Snippet: The primary polyclonal rabbit antibodies, used at a 1:2500 dilution, were anti-MMP 2 (hinge region), anti-MMP 3 (hinge region), anti-MMP 9 (N-terminal region of the active form), anti-TIMP 1 (C-terminal region), anti-TIMP 2, and anti-TIMP 3 (Chemicon, Temecula, CA).

    Techniques: Immunohistochemistry, Labeling, Amplification, Staining, Marker, Expressing

    Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in adult rat cerebellar cortex. Ten micrometer frontal sections of adult rat cerebellum showed the EGL, the ML, the PCL, and the IGL. Labeling with polyclonal antibodies was amplified by using tyramide signal amplification (New England Nuclear). Note, for each marker, the cytoplasmic staining at the adult age compared with the diffuse staining seen on the developmental stages P10 and P15. In the ML, MMPs 3 and 9 and TIMPs 1, 2, and 3 protein expression was lost in PK cell arborization. However, MMP 9 expression persisted in the Bergmann glial fibers. Double arrows point to one fiber in C . Only the anti-TIMP 3 antibodies labeled PK cells dendrites. Arrow indicates TIMP 3 dendritic immunolabeling in F . Interneurons of the ML were labeled for MMPs 3 and 9 and TIMPs 1 and 2. In the PCL, all markers were detected in PK cell somata. In addition, MMP 9 and TIMP 1 were seen in the Bergmann glial cell bodies surrounding the PK cell somata. In the IGL, MMPs 3 and 9 and TIMPs 2 and 3 were strongly expressed in many granular cells, whereas TIMP 1 was poorly expressed. Magnification of the left of each panel, 100×. Magnification of the right of each panel, 400×. Scale bars, 100 μm.

    Journal: The Journal of Neuroscience

    Article Title: Spatiotemporal Expression Patterns of Metalloproteinases and Their Inhibitors in the Postnatal Developing Rat Cerebellum

    doi: 10.1523/JNEUROSCI.19-12-04994.1999

    Figure Lengend Snippet: Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in adult rat cerebellar cortex. Ten micrometer frontal sections of adult rat cerebellum showed the EGL, the ML, the PCL, and the IGL. Labeling with polyclonal antibodies was amplified by using tyramide signal amplification (New England Nuclear). Note, for each marker, the cytoplasmic staining at the adult age compared with the diffuse staining seen on the developmental stages P10 and P15. In the ML, MMPs 3 and 9 and TIMPs 1, 2, and 3 protein expression was lost in PK cell arborization. However, MMP 9 expression persisted in the Bergmann glial fibers. Double arrows point to one fiber in C . Only the anti-TIMP 3 antibodies labeled PK cells dendrites. Arrow indicates TIMP 3 dendritic immunolabeling in F . Interneurons of the ML were labeled for MMPs 3 and 9 and TIMPs 1 and 2. In the PCL, all markers were detected in PK cell somata. In addition, MMP 9 and TIMP 1 were seen in the Bergmann glial cell bodies surrounding the PK cell somata. In the IGL, MMPs 3 and 9 and TIMPs 2 and 3 were strongly expressed in many granular cells, whereas TIMP 1 was poorly expressed. Magnification of the left of each panel, 100×. Magnification of the right of each panel, 400×. Scale bars, 100 μm.

    Article Snippet: The primary polyclonal rabbit antibodies, used at a 1:2500 dilution, were anti-MMP 2 (hinge region), anti-MMP 3 (hinge region), anti-MMP 9 (N-terminal region of the active form), anti-TIMP 1 (C-terminal region), anti-TIMP 2, and anti-TIMP 3 (Chemicon, Temecula, CA).

    Techniques: Immunohistochemistry, Labeling, Amplification, Marker, Staining, Expressing, Immunolabeling

    Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in the cerebellar cortex of 15-d-old rats. Ten-micrometer-thick frontal sections of rat cerebellum showed the EGL, the ML, the PCL, and the IGL. Immunohistochemical staining was performed using polyclonal antibodies and amplified by tyramide signal amplification (New England Nuclear). EGL immunostaining for MMPs 3 and 9 and TIMPs 1, 2, and 3 was lost. The PK cell dendrites were still stained for MMP 3 and TIMP 3. Note the diffuse extracellular distribution of MMP 3 as opposed to the cytoplasmic distribution of TIMP 3. ML labeling for MMP 9 and TIMP 1 in the PK cell dendrites decreased, but MMP 9 labeling of Bergmann glial fibers was maintained. MMP 9 labeling in ML cells, probably corresponding to stellate and basket cells, was detected. The large double arrows point to MMP 9-positive Bergmann glial fibers, and the small arrows point to MMP 9-positive ML cells ( C ). In the PCL, expression of MMPs 2, 3, and 9 and TIMPs 1, 2, and 3 was noted in the PK cell somata. TIMP 1 was differentially expressed in clusters of PK cell somata (stained and unstained PK cell somata are respectively indicated by large arrows at the left and right of D ). TIMP 1 was also present in Bergmann glial somata around labeled and unlabeled PK cell bodies ( D ). Granular cells in the IGL were positive for MMPs 3 and 9 and TIMPs 1 and 3. Scale bar, 25 μm.

    Journal: The Journal of Neuroscience

    Article Title: Spatiotemporal Expression Patterns of Metalloproteinases and Their Inhibitors in the Postnatal Developing Rat Cerebellum

    doi: 10.1523/JNEUROSCI.19-12-04994.1999

    Figure Lengend Snippet: Immunohistochemical distribution pattern of MMP 2 ( A ), MMP 3 ( B ), MMP 9 ( C ), TIMP 1 ( D ), TIMP 2 ( E ), and TIMP 3 ( F ) in the cerebellar cortex of 15-d-old rats. Ten-micrometer-thick frontal sections of rat cerebellum showed the EGL, the ML, the PCL, and the IGL. Immunohistochemical staining was performed using polyclonal antibodies and amplified by tyramide signal amplification (New England Nuclear). EGL immunostaining for MMPs 3 and 9 and TIMPs 1, 2, and 3 was lost. The PK cell dendrites were still stained for MMP 3 and TIMP 3. Note the diffuse extracellular distribution of MMP 3 as opposed to the cytoplasmic distribution of TIMP 3. ML labeling for MMP 9 and TIMP 1 in the PK cell dendrites decreased, but MMP 9 labeling of Bergmann glial fibers was maintained. MMP 9 labeling in ML cells, probably corresponding to stellate and basket cells, was detected. The large double arrows point to MMP 9-positive Bergmann glial fibers, and the small arrows point to MMP 9-positive ML cells ( C ). In the PCL, expression of MMPs 2, 3, and 9 and TIMPs 1, 2, and 3 was noted in the PK cell somata. TIMP 1 was differentially expressed in clusters of PK cell somata (stained and unstained PK cell somata are respectively indicated by large arrows at the left and right of D ). TIMP 1 was also present in Bergmann glial somata around labeled and unlabeled PK cell bodies ( D ). Granular cells in the IGL were positive for MMPs 3 and 9 and TIMPs 1 and 3. Scale bar, 25 μm.

    Article Snippet: The primary polyclonal rabbit antibodies, used at a 1:2500 dilution, were anti-MMP 2 (hinge region), anti-MMP 3 (hinge region), anti-MMP 9 (N-terminal region of the active form), anti-TIMP 1 (C-terminal region), anti-TIMP 2, and anti-TIMP 3 (Chemicon, Temecula, CA).

    Techniques: Immunohistochemistry, Staining, Amplification, Immunostaining, Labeling, Expressing

    Anti-hsp90 antibodies increase NadA Δ351–405 monocyte stimulation in a polymixin B insensitive-way. A) Cells were treated with NadA Δ351–405 in the absence (black circles) or in the presence (open circles) of purified rabbit polyclonal antibodies directed to the COOH terminal domain of hsp90. Open squares refers to cells incubated with NadA Δ351–405 in the presence of purified rabbit polyclonal antibodies from non immunized animals. The indicated cytokines/chemokines were analyzed in the extracellular medium by BioPlex suspension arrays. Data are the mean from a representative experiment out of four run in triplicate. Bars are +/− SE. Asterisk indicates signals significantly different (p

    Journal: PLoS ONE

    Article Title: The Soluble Recombinant Neisseria meningitidis Adhesin NadAΔ351–405 Stimulates Human Monocytes by Binding to Extracellular Hsp90

    doi: 10.1371/journal.pone.0025089

    Figure Lengend Snippet: Anti-hsp90 antibodies increase NadA Δ351–405 monocyte stimulation in a polymixin B insensitive-way. A) Cells were treated with NadA Δ351–405 in the absence (black circles) or in the presence (open circles) of purified rabbit polyclonal antibodies directed to the COOH terminal domain of hsp90. Open squares refers to cells incubated with NadA Δ351–405 in the presence of purified rabbit polyclonal antibodies from non immunized animals. The indicated cytokines/chemokines were analyzed in the extracellular medium by BioPlex suspension arrays. Data are the mean from a representative experiment out of four run in triplicate. Bars are +/− SE. Asterisk indicates signals significantly different (p

    Article Snippet: No E. coli Ags were detected by Western immunoblot analysis with a rabbit polyclonal Ab risen against whole E. coli cells (DakoCytomation).

    Techniques: Purification, Incubation

    CDX2 immunolabelling controls. The binding specificity of the rabbit polyclonal anti CDX2 primary antibody (ab88129) (a) and mouse monoclonal anti CDX2 primary antibody (ab15258) (b) was verified with the use of blocking peptide (ab99158) prior to the antibody staining. The secondary antibodies used were goat anti-rabbit Rhodamine conjugated (sc-2091) in (a) and goat anti-mouse Rhodamine conjugated (sc-2092) in (b) . Dashed circle marks the metaphase plate. DAPI labels chromatin.

    Journal: BMC Developmental Biology

    Article Title: Changes in sub-cellular localisation of trophoblast and inner cell mass specific transcription factors during bovine preimplantation development

    doi: 10.1186/1471-213X-13-32

    Figure Lengend Snippet: CDX2 immunolabelling controls. The binding specificity of the rabbit polyclonal anti CDX2 primary antibody (ab88129) (a) and mouse monoclonal anti CDX2 primary antibody (ab15258) (b) was verified with the use of blocking peptide (ab99158) prior to the antibody staining. The secondary antibodies used were goat anti-rabbit Rhodamine conjugated (sc-2091) in (a) and goat anti-mouse Rhodamine conjugated (sc-2092) in (b) . Dashed circle marks the metaphase plate. DAPI labels chromatin.

    Article Snippet: The primary antibody set included: anti-CDX2 - mouse monoclonal AB (Abcam, UK, ab15258) or rabbit polyclonal AB (Abcam, ab88129); anti-OCT4 rabbit polyclonal AB (Abcam, ab18976) or goat polyclonal AB (Abcam, ab27985); anti-NANOG rabbit polyclonal AB (PeproTech, UK, 500-P236), anti-trimethyl-histone H3 (Lys9) AB (Merck-Millipore, 07–442).

    Techniques: Binding Assay, Blocking Assay, Staining

    OCT4 immunolabelling controls. Control immunostaining with both of the anti OCT4 antibodies used in the experiment. (a1) presents HBL single labelled for OCT4 with goat polyclonal primary antibody (ab27985) detected with mouse anti-goat Rhodamine conjugated secondary antibody (sc-24900). (a2) presents single labelled HBl with rabbit polyclonal anti OCT4 antibody (ab18976) detected with goat anti-rabbit FITC conjugated secondary antibody (sc-2012). (b) indicates colocalisation of the OCT4 in HBl double-labelled with both of the anti OCT4 antibodies. The secondary antibodies used were mouse anti-goat Rhodamine conjugated (sc-2490) and donkey anti-rabbit FITC conjugated (sc-2090). DAPI labels chromatin.

    Journal: BMC Developmental Biology

    Article Title: Changes in sub-cellular localisation of trophoblast and inner cell mass specific transcription factors during bovine preimplantation development

    doi: 10.1186/1471-213X-13-32

    Figure Lengend Snippet: OCT4 immunolabelling controls. Control immunostaining with both of the anti OCT4 antibodies used in the experiment. (a1) presents HBL single labelled for OCT4 with goat polyclonal primary antibody (ab27985) detected with mouse anti-goat Rhodamine conjugated secondary antibody (sc-24900). (a2) presents single labelled HBl with rabbit polyclonal anti OCT4 antibody (ab18976) detected with goat anti-rabbit FITC conjugated secondary antibody (sc-2012). (b) indicates colocalisation of the OCT4 in HBl double-labelled with both of the anti OCT4 antibodies. The secondary antibodies used were mouse anti-goat Rhodamine conjugated (sc-2490) and donkey anti-rabbit FITC conjugated (sc-2090). DAPI labels chromatin.

    Article Snippet: The primary antibody set included: anti-CDX2 - mouse monoclonal AB (Abcam, UK, ab15258) or rabbit polyclonal AB (Abcam, ab88129); anti-OCT4 rabbit polyclonal AB (Abcam, ab18976) or goat polyclonal AB (Abcam, ab27985); anti-NANOG rabbit polyclonal AB (PeproTech, UK, 500-P236), anti-trimethyl-histone H3 (Lys9) AB (Merck-Millipore, 07–442).

    Techniques: Immunostaining

    Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit polyclonal Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Integration of Runx and Smad regulatory signals at transcriptionally active subnuclear sites

    doi: 10.1073/pnas.112664499

    Figure Lengend Snippet: Runx2 transcription factor targets Smads to subnuclear sites. HeLa cells, which lack endogenous Runx proteins, were transfected with 0.5 μg of expression construct for Flag Smad5 together with HA-Runx2 expression vector. BMP2-treated or untreated cells were processed for WC ( a – c , untreated cells; g – i , BMP2-treated cells) or NM-IF ( d – f , untreated cells; j – l , BMP2-treated cells) preparation and in situ immunofluorescence 24 h after transfection. Smad5 was detected with mouse mAb against Flag tag whereas Runx2 was detected by a rabbit polyclonal Ab against HA tag. To confirm that the activation of Smad5 by BMP2 is required for nuclear accumulation and consequent subnuclear targeting of Smad5, a dominant negative inhibitor of BMP signaling, BMPRI (KR), was expressed along with expression constructs for HA-Runx2 and Flag-Smad5. Cells were treated with BMP2 and were processed for WC ( m – o ) or NM-IF ( p – r ) preparation and in situ immunofluorescence as described.

    Article Snippet: Runx2 was detected by a rabbit polyclonal Ab against the HA tag at a dilution of 1:3000 (Santa Cruz Biotechnology).

    Techniques: Transfection, Expressing, Construct, Plasmid Preparation, In Situ, Immunofluorescence, FLAG-tag, Activation Assay, Dominant Negative Mutation, IF-P

    Runx factors specify subnuclear localization of Smads. HeLa cells were transfected with 0.5 μg of expression construct for Flag Smad1 along with Runx1, Runx2, or Runx3 expression vectors. Cells were treated with BMP2, and Smad1 was examined for association with Runx factors in the nuclear matrix (NM-IF preparation) by in situ immunofluorescence 24 h after transfection. Smad1 was detected with mouse mAb against Flag tag. Runx proteins were detected with rabbit polyclonal Abs at a dilution of 1:200. Images were taken by a Zeiss Axioplan microscope coupled with a charge-coupled device (CCD) camera and were processed for deconvulation microscopy with METAMORPH bioimaging software.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Integration of Runx and Smad regulatory signals at transcriptionally active subnuclear sites

    doi: 10.1073/pnas.112664499

    Figure Lengend Snippet: Runx factors specify subnuclear localization of Smads. HeLa cells were transfected with 0.5 μg of expression construct for Flag Smad1 along with Runx1, Runx2, or Runx3 expression vectors. Cells were treated with BMP2, and Smad1 was examined for association with Runx factors in the nuclear matrix (NM-IF preparation) by in situ immunofluorescence 24 h after transfection. Smad1 was detected with mouse mAb against Flag tag. Runx proteins were detected with rabbit polyclonal Abs at a dilution of 1:200. Images were taken by a Zeiss Axioplan microscope coupled with a charge-coupled device (CCD) camera and were processed for deconvulation microscopy with METAMORPH bioimaging software.

    Article Snippet: Runx2 was detected by a rabbit polyclonal Ab against the HA tag at a dilution of 1:3000 (Santa Cruz Biotechnology).

    Techniques: Transfection, Expressing, Construct, In Situ, Immunofluorescence, FLAG-tag, Microscopy, Software

    Runx2 is required for subnuclear targeting of Smad5. ( a ) A schematic of Runx2 protein. The region where Smads interact is shown. The Y428A mutation, which disrupts association of Runx2 with the nuclear matrix, was introduced by PCR-based site-directed mutagenesis. QA, poly glutamine-poly alanine stretch; RHD, runt homology domain; NMTS, nuclear matrix-targeting signal; VWRPY, a highly conserved motif that mediate interactions of Runx2 with groucho /TLE proteins. ( b ) ROS17/2.8 cells grown in 100-mm plates were transfected with 10 μg each of expression constructs for Flag-Smad1 and wild-type HA-Runx2 or HA-Runx2 Y428A mutant. Cells were treated with 300 ng/ml of BMP2 for 24 h and processed for immunoprecipitation. One microgram Ab against Flag tag was used for immunoprecipitation. The immunoprecipitated complex was resolved by 8% SDS/PAGE. Wild-type or mutant Runx2 proteins were detected with mouse mAb against HA tag (dilution 1:2000). HeLa cells were transfected with 0.5 μg of expression constructs for Flag-Smad1 along with HA-tagged wild-type or Runx2 Y428A mutant proteins. Cells were treated with BMP2 and subjected to WC ( c – e ) or NM-IF ( f – h ) preparation and double-labeled in situ immunofluorescence with mouse mAb against Flag tag and rabbit polyclonal Ab against HA tag.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Integration of Runx and Smad regulatory signals at transcriptionally active subnuclear sites

    doi: 10.1073/pnas.112664499

    Figure Lengend Snippet: Runx2 is required for subnuclear targeting of Smad5. ( a ) A schematic of Runx2 protein. The region where Smads interact is shown. The Y428A mutation, which disrupts association of Runx2 with the nuclear matrix, was introduced by PCR-based site-directed mutagenesis. QA, poly glutamine-poly alanine stretch; RHD, runt homology domain; NMTS, nuclear matrix-targeting signal; VWRPY, a highly conserved motif that mediate interactions of Runx2 with groucho /TLE proteins. ( b ) ROS17/2.8 cells grown in 100-mm plates were transfected with 10 μg each of expression constructs for Flag-Smad1 and wild-type HA-Runx2 or HA-Runx2 Y428A mutant. Cells were treated with 300 ng/ml of BMP2 for 24 h and processed for immunoprecipitation. One microgram Ab against Flag tag was used for immunoprecipitation. The immunoprecipitated complex was resolved by 8% SDS/PAGE. Wild-type or mutant Runx2 proteins were detected with mouse mAb against HA tag (dilution 1:2000). HeLa cells were transfected with 0.5 μg of expression constructs for Flag-Smad1 along with HA-tagged wild-type or Runx2 Y428A mutant proteins. Cells were treated with BMP2 and subjected to WC ( c – e ) or NM-IF ( f – h ) preparation and double-labeled in situ immunofluorescence with mouse mAb against Flag tag and rabbit polyclonal Ab against HA tag.

    Article Snippet: Runx2 was detected by a rabbit polyclonal Ab against the HA tag at a dilution of 1:3000 (Santa Cruz Biotechnology).

    Techniques: Mutagenesis, Polymerase Chain Reaction, Transfection, Expressing, Construct, Immunoprecipitation, FLAG-tag, SDS Page, Labeling, In Situ, Immunofluorescence

    Representative Western blots showing the time course of cyclin D1, E, and A protein expression induced by FCS (10%) in cultured rat aortic smooth muscle cells. Equal amounts of protein from nuclear extracts were subjected to SDS–PAGE, transferred to nitrocellulose membranes, and immunoblotted with polyclonal antibodies against G1 phase cyclin D1 (top), and cyclin E (center) and S phase cyclin A (bottom). Similar results were obtained in two additional experiments.

    Journal: British Journal of Pharmacology

    Article Title: Growth-inhibitory effect of cyclic GMP- and cyclic AMP-dependent vasodilators on rat vascular smooth muscle cells: effect on cell cycle and cyclin expression

    doi: 10.1038/sj.bjp.0702305

    Figure Lengend Snippet: Representative Western blots showing the time course of cyclin D1, E, and A protein expression induced by FCS (10%) in cultured rat aortic smooth muscle cells. Equal amounts of protein from nuclear extracts were subjected to SDS–PAGE, transferred to nitrocellulose membranes, and immunoblotted with polyclonal antibodies against G1 phase cyclin D1 (top), and cyclin E (center) and S phase cyclin A (bottom). Similar results were obtained in two additional experiments.

    Article Snippet: The immobilized cyclin D1, E and A proteins were detected by subsequent incubation with polyclonal rabbit antibodies directed against cyclin D1, E and A, respectively, (dilution 1 : 1000, overnight at 4°C; Santa Cruz, Heidelberg, Germany) and then with a secondary polyclonal donkey anti-rabbit immunoglobulin antibody conjugated to horseradish peroxidase (dilution 1 : 10,000, 1 h at 22°C; Calbiochem).

    Techniques: Western Blot, Expressing, Cell Culture, SDS Page