rabbit polyclonal Search Results


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  • 99
    Thermo Fisher gfp tag polyclonal antibody
    Gfp Tag Polyclonal Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 8757 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rabbit polyclonal antibody
    Rabbit Polyclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 7185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit polyclonal antibody
    Rabbit Polyclonal Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 11154 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal antibody
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Rabbit Polyclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 10603 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit polyclonal
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Rabbit Polyclonal, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 8602 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore polyclonal antibodies
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Polyclonal Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2847 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Cell Signaling Technology Inc rabbit polyclonal antibody
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Rabbit Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 5570 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam goat anti rabbit igg h l hrp
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Goat Anti Rabbit Igg H L Hrp, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 2991 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rabbit polyclonal antibodies
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Rabbit Polyclonal Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2715 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rabbit polyclonal antibody
    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using <t>polyclonal</t> antibodies to the myc- and HA-tags.
    Rabbit Polyclonal Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2922 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti histone h3 antibody nuclear loading control and chip grade
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Anti Histone H3 Antibody Nuclear Loading Control And Chip Grade, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1336 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Proteintech rabbit gapdh polyclonal
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Rabbit Gapdh Polyclonal, supplied by Proteintech, used in various techniques. Bioz Stars score: 99/100, based on 1654 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Rabbit Polyclonal, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 2880 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    gapdh  (Abcam)
    99
    Abcam gapdh
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Gapdh, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 18820 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti histone h3 acetyl k27 antibody chip grade
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Anti Histone H3 Acetyl K27 Antibody Chip Grade, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 840 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rabbit polyclonal antibodies
    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes
    Rabbit Polyclonal Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1454 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti cd31 antibody
    RNA sequencing (RNA-seq) assay shows mesenchymal-endothelial transition (MEndoT)-derived cells are more endothelial-like after cardiac hypertrophy but may be a different cell sub-population. Non-myocytes were isolated from hearts of 14 day post-sham or -transverse aortic constriction (TAC) in Col1a2-CreERT: R26R tdTomato mice and native fibroblasts (tdTomato + -labeled fibroblasts after sham-injury), MEndoT-derived cells (tdTomato + <t>CD31</t> + -labeled cells) were collected using flow cytometry for RNA-seq. The tdTomato + -labeled endothelial cells from heart tissue of Tek-CreERT: R26R tdTomato mice after sham injury were collected and served as native coronary endothelial cells. ( a ) Principal component analysis clustering show MEndoT-derived cells are a subset cell population with characteristics that were closer to native endothelial cells than native fibroblasts. ( b ) p53 is specifically and significantly upregulated in MEndoT-derived cells. Heatmap show significantly expressed genes indicative of ( c ) fibroblast lineage commitment and ( d ) endothelial lineage commitment (all genes in b-d have a q-value
    Anti Cd31 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1561 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: MT cosedimentation of HC expressed with the LC deletion mutants. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC alone ( H ), HC and LC ( H + L ), or HC and the LC deletion mutants ( H + L176 , H + L237 , H + L405 , and H + L488 ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Expressing

    MT cosedimentation of expressed recombinant HC+LC and endogenous kinesin is pH dependent. ( A ) Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC ( H ) or HC and LC ( H + L ). Lysates were prepared in LB+Triton X-100 buffered with MES (pH 6.4), Pipes (pH 6.8), or Hepes (pH 7.2 and 7.6). MTs and bound proteins were sedimented through a sucrose cushion and the MT pellets and supernatants were immunoblotted with antibodies against myc- and HA-epitope tags to detect the expressed recombinant proteins. Only the immunoblots of the MT pellets are shown. ( B ) The pH dependence of MT binding of HC alone ( circles ) or HC and LC ( triangles ) was determined between pH 6.8 and 7.2 in LB + Triton X-100 buffered with Pipes ( solid line ) or Hepes ( dashed line ). Each data point represents the mean ± SD of at least five separate experiments. ( C ) Taxol-stabilized MTs and AMP-PNP were added to lysates, prepared at pH 6.8 or 7.2 as in A , from COS cells coexpressing the indicated recombinant proteins. MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags. ( D ) Sedimentation analysis of coexpressed HC and LC. COS cell lysates made at pH 6.8 ( circles ) and 7.2 ( squares ) were subjected to sedimentation on linear 9–15% sucrose gradients, both at physiological ( closed symbols ) and high salt (0.5 M NaCl; open symbols ) concentrations. The expressed recombinant proteins were detected in the fractions by immunoblotting with polyclonal antibodies to the myc- and HA-tags. The mobility on the gradient of proteins with known S values is indicated. ( E ) Taxol-stabilized MTs and AMP-PNP were added to lysates, prepared at pH 6.8 or 7.2 as in A , from untransfected COS cells. MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect endogenous kinesin using a polyclonal antibody to kinesin HC.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: MT cosedimentation of expressed recombinant HC+LC and endogenous kinesin is pH dependent. ( A ) Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC ( H ) or HC and LC ( H + L ). Lysates were prepared in LB+Triton X-100 buffered with MES (pH 6.4), Pipes (pH 6.8), or Hepes (pH 7.2 and 7.6). MTs and bound proteins were sedimented through a sucrose cushion and the MT pellets and supernatants were immunoblotted with antibodies against myc- and HA-epitope tags to detect the expressed recombinant proteins. Only the immunoblots of the MT pellets are shown. ( B ) The pH dependence of MT binding of HC alone ( circles ) or HC and LC ( triangles ) was determined between pH 6.8 and 7.2 in LB + Triton X-100 buffered with Pipes ( solid line ) or Hepes ( dashed line ). Each data point represents the mean ± SD of at least five separate experiments. ( C ) Taxol-stabilized MTs and AMP-PNP were added to lysates, prepared at pH 6.8 or 7.2 as in A , from COS cells coexpressing the indicated recombinant proteins. MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags. ( D ) Sedimentation analysis of coexpressed HC and LC. COS cell lysates made at pH 6.8 ( circles ) and 7.2 ( squares ) were subjected to sedimentation on linear 9–15% sucrose gradients, both at physiological ( closed symbols ) and high salt (0.5 M NaCl; open symbols ) concentrations. The expressed recombinant proteins were detected in the fractions by immunoblotting with polyclonal antibodies to the myc- and HA-tags. The mobility on the gradient of proteins with known S values is indicated. ( E ) Taxol-stabilized MTs and AMP-PNP were added to lysates, prepared at pH 6.8 or 7.2 as in A , from untransfected COS cells. MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect endogenous kinesin using a polyclonal antibody to kinesin HC.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Recombinant, Expressing, Western Blot, Binding Assay, Sedimentation

    MT cosedimentation of the HC deletion mutants expressed alone or together with LC. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC ( H ) or the deletion mutants ( H682 , H810 , and H891 ) alone or together with LC ( H + L , H682 + L , H810 + L , and H891 + L ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: MT cosedimentation of the HC deletion mutants expressed alone or together with LC. Taxol-stabilized MTs and AMP-PNP were added to lysates from COS cells expressing HC ( H ) or the deletion mutants ( H682 , H810 , and H891 ) alone or together with LC ( H + L , H682 + L , H810 + L , and H891 + L ). MTs and bound proteins were sedimented through a sucrose cushion. The MT pellets ( P ) and supernatants ( S ) were immunoblotted to detect the expressed proteins using polyclonal antibodies to the myc- and HA-tags.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Expressing

    Interaction of the LC deletion mutants with HC. ( A ) Deletion mutants of LC were constructed in which stop codons were engineered after amino acids 176, 237, 405, and 488. These constructs retain the heptad repeat region but contain deletions of some or all of the TPR motifs. The deletion mutant LΔHR is missing only the heptad repeat region. Amino acids numbers for the full length protein are shown below the schematic of LC. ( B ) COS cells expressing HC, LC, or the LC deletion mutants alone (H, L, L176, L237, L405, L488, LΔHR; top ) or expressing HC together with LC or the LC deletion mutants ( H + L , H + L176 , H + L237 , H + L405 , H + L488 , and H + LΔHR ; bottom ) were lysed with 1% Triton X-100. After centrifugation, the amount of expressed protein found insoluble in the pellet ( P ) and soluble in the lysate ( S ) was determined by immunoblotting with polyclonal antibodies to the myc- and HA-epitope tags. Molecular weight size standards (kilodaltons) are indicated on the left. ( C ) Coimmunoprecipitation of HC and the LC deletion mutants. Lysates were immunoprecipitated for HC using a monoclonal anti–myc antibody ( left ) or for LC using a monoclonal anti–HA antibody ( right ). Immunoprecipitates were immunoblotted to detect the expressed proteins using polyclonal antibodies to the epitope tags.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: Interaction of the LC deletion mutants with HC. ( A ) Deletion mutants of LC were constructed in which stop codons were engineered after amino acids 176, 237, 405, and 488. These constructs retain the heptad repeat region but contain deletions of some or all of the TPR motifs. The deletion mutant LΔHR is missing only the heptad repeat region. Amino acids numbers for the full length protein are shown below the schematic of LC. ( B ) COS cells expressing HC, LC, or the LC deletion mutants alone (H, L, L176, L237, L405, L488, LΔHR; top ) or expressing HC together with LC or the LC deletion mutants ( H + L , H + L176 , H + L237 , H + L405 , H + L488 , and H + LΔHR ; bottom ) were lysed with 1% Triton X-100. After centrifugation, the amount of expressed protein found insoluble in the pellet ( P ) and soluble in the lysate ( S ) was determined by immunoblotting with polyclonal antibodies to the myc- and HA-epitope tags. Molecular weight size standards (kilodaltons) are indicated on the left. ( C ) Coimmunoprecipitation of HC and the LC deletion mutants. Lysates were immunoprecipitated for HC using a monoclonal anti–myc antibody ( left ) or for LC using a monoclonal anti–HA antibody ( right ). Immunoprecipitates were immunoblotted to detect the expressed proteins using polyclonal antibodies to the epitope tags.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Construct, Mutagenesis, Expressing, Centrifugation, Molecular Weight, Immunoprecipitation

    Localization of HC expressed with the LC deletion mutants. COS cells were transiently transfected with plasmids encoding the indicated proteins and the expressed proteins were localized by immunofluorescence microscopy. HC was detected with anti–myc monoclonal and Rhodamine Red-X–labeled anti–mouse secondary antibodies. The LC deletion mutants were detected with anti–HA polyclonal and Oregon green 488–labeled anti–rabbit secondary antibodies. For coexpression of HC with L488, note that the cell on the left expresses both proteins and shows diffuse staining, whereas the cell on the right expresses only HC and shows MT staining ( G and H ). Bar, 10 μm.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: Localization of HC expressed with the LC deletion mutants. COS cells were transiently transfected with plasmids encoding the indicated proteins and the expressed proteins were localized by immunofluorescence microscopy. HC was detected with anti–myc monoclonal and Rhodamine Red-X–labeled anti–mouse secondary antibodies. The LC deletion mutants were detected with anti–HA polyclonal and Oregon green 488–labeled anti–rabbit secondary antibodies. For coexpression of HC with L488, note that the cell on the left expresses both proteins and shows diffuse staining, whereas the cell on the right expresses only HC and shows MT staining ( G and H ). Bar, 10 μm.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Transfection, Immunofluorescence, Microscopy, Labeling, Staining

    Interaction of the HC deletion mutants with LC. ( A ) Deletion mutants of HC were constructed in which stop codons were engineered after amino acids 682, 810, and 891. These deletions remove both the tail domain and the conserved region of the stalk domain ( H682 ), the entire tail domain ( H810 ), or half of the tail domain ( H891 ). ( B ) COS cells expressing HC or the HC deletion mutants alone ( H , H682 , H810 , and H891 ; top ) or together with LC ( H + L , H682 + L , H810 + L , and H891 + L ; bottom ) were lysed with 1% Triton X-100. After centrifugation, the amount of expressed protein found insoluble in the pellet ( P ) and soluble in the lysate ( S ) was determined by immunoblotting with polyclonal antibodies to the myc- and HA-epitope tags. Molecular weight size standards (kilodaltons) are indicated on the left. ( C ) Coimmunoprecipitation of the HC deletion mutants and LC. Lysates were immunoprecipitated for HC using a monoclonal anti–myc antibody ( left ) or for LC using a monoclonal anti–HA antibody ( right ). Immunoprecipitates were immunoblotted to detect the expressed proteins using polyclonal antibodies to the epitope tags.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: Interaction of the HC deletion mutants with LC. ( A ) Deletion mutants of HC were constructed in which stop codons were engineered after amino acids 682, 810, and 891. These deletions remove both the tail domain and the conserved region of the stalk domain ( H682 ), the entire tail domain ( H810 ), or half of the tail domain ( H891 ). ( B ) COS cells expressing HC or the HC deletion mutants alone ( H , H682 , H810 , and H891 ; top ) or together with LC ( H + L , H682 + L , H810 + L , and H891 + L ; bottom ) were lysed with 1% Triton X-100. After centrifugation, the amount of expressed protein found insoluble in the pellet ( P ) and soluble in the lysate ( S ) was determined by immunoblotting with polyclonal antibodies to the myc- and HA-epitope tags. Molecular weight size standards (kilodaltons) are indicated on the left. ( C ) Coimmunoprecipitation of the HC deletion mutants and LC. Lysates were immunoprecipitated for HC using a monoclonal anti–myc antibody ( left ) or for LC using a monoclonal anti–HA antibody ( right ). Immunoprecipitates were immunoblotted to detect the expressed proteins using polyclonal antibodies to the epitope tags.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Construct, Expressing, Centrifugation, Molecular Weight, Immunoprecipitation

    Localization of HC expressed alone, LC expressed alone, and HC and LC expressed together. COS cells were transiently transfected with plasmids encoding HC alone ( A–D ), LC alone ( E and F ) or both HC and LC ( G–J ). The expressed proteins were localized by immunofluorescence microscopy. ( A and B ) HC was detected with an anti–myc monoclonal antibody followed by Rhodamine Red-X–labeled anti–mouse secondary antibody. ( C and D ) Cells were double labeled for HC and MTs. HC was detected with anti–myc polyclonal and Oregon green 488–labeled anti–rabbit antibodies, and tubulin was detected with antitubulin monoclonal and Rhodamine Red-X–labeled anti–mouse secondary antibodies. ( E and F ) LC was detected with anti–HA polyclonal and Oregon green 488–labeled anti–rabbit secondary antibodies. ( G–J ) Cells were double labeled for HC and LC. HC was detected with anti–myc monoclonal and Rhodamine Red-X–labeled anti–mouse antibodies, and LC was detected with anti–HA polyclonal and Oregon green 488– labeled anti–rabbit secondary antibodies. Bar, 10 μm.

    Journal: The Journal of Cell Biology

    Article Title: Light Chain- dependent Regulation of Kinesin's Interaction with Microtubules

    doi:

    Figure Lengend Snippet: Localization of HC expressed alone, LC expressed alone, and HC and LC expressed together. COS cells were transiently transfected with plasmids encoding HC alone ( A–D ), LC alone ( E and F ) or both HC and LC ( G–J ). The expressed proteins were localized by immunofluorescence microscopy. ( A and B ) HC was detected with an anti–myc monoclonal antibody followed by Rhodamine Red-X–labeled anti–mouse secondary antibody. ( C and D ) Cells were double labeled for HC and MTs. HC was detected with anti–myc polyclonal and Oregon green 488–labeled anti–rabbit antibodies, and tubulin was detected with antitubulin monoclonal and Rhodamine Red-X–labeled anti–mouse secondary antibodies. ( E and F ) LC was detected with anti–HA polyclonal and Oregon green 488–labeled anti–rabbit secondary antibodies. ( G–J ) Cells were double labeled for HC and LC. HC was detected with anti–myc monoclonal and Rhodamine Red-X–labeled anti–mouse antibodies, and LC was detected with anti–HA polyclonal and Oregon green 488– labeled anti–rabbit secondary antibodies. Bar, 10 μm.

    Article Snippet: Rabbit polyclonal antibodies to the myc- and HA-tags were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Transfection, Immunofluorescence, Microscopy, Labeling

    Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes

    Journal: Virology

    Article Title: Curcumin inhibits herpes simplex virus immediate-early gene expression by a mechanism independent of p300/CBP histone acetyltransferase activity

    doi: 10.1016/j.virol.2007.11.028

    Figure Lengend Snippet: Curcumin does not affect histone H3, p300, or CBP occupancy, nor H3 acetylation, at IE genes

    Article Snippet: ChIP assays were performed using antibodies or antisera directed against VP16 , RNA Pol II (8WG16; Covance), CBP (A-22; Santa Cruz Biotechnology), p300 (N-15; Santa Cruz Biotechnology), histone H3 acetylated at Lys9 (07-352, Upstate), histone H3 acetylated at Lys14 (07-353, Upstate) and a C-terminal epitope of histone H3 (ab1791; Abcam).

    Techniques:

    RNA sequencing (RNA-seq) assay shows mesenchymal-endothelial transition (MEndoT)-derived cells are more endothelial-like after cardiac hypertrophy but may be a different cell sub-population. Non-myocytes were isolated from hearts of 14 day post-sham or -transverse aortic constriction (TAC) in Col1a2-CreERT: R26R tdTomato mice and native fibroblasts (tdTomato + -labeled fibroblasts after sham-injury), MEndoT-derived cells (tdTomato + CD31 + -labeled cells) were collected using flow cytometry for RNA-seq. The tdTomato + -labeled endothelial cells from heart tissue of Tek-CreERT: R26R tdTomato mice after sham injury were collected and served as native coronary endothelial cells. ( a ) Principal component analysis clustering show MEndoT-derived cells are a subset cell population with characteristics that were closer to native endothelial cells than native fibroblasts. ( b ) p53 is specifically and significantly upregulated in MEndoT-derived cells. Heatmap show significantly expressed genes indicative of ( c ) fibroblast lineage commitment and ( d ) endothelial lineage commitment (all genes in b-d have a q-value

    Journal: Scientific Reports

    Article Title: Mesenchymal-endothelial transition-derived cells as a potential new regulatory target for cardiac hypertrophy

    doi: 10.1038/s41598-020-63671-8

    Figure Lengend Snippet: RNA sequencing (RNA-seq) assay shows mesenchymal-endothelial transition (MEndoT)-derived cells are more endothelial-like after cardiac hypertrophy but may be a different cell sub-population. Non-myocytes were isolated from hearts of 14 day post-sham or -transverse aortic constriction (TAC) in Col1a2-CreERT: R26R tdTomato mice and native fibroblasts (tdTomato + -labeled fibroblasts after sham-injury), MEndoT-derived cells (tdTomato + CD31 + -labeled cells) were collected using flow cytometry for RNA-seq. The tdTomato + -labeled endothelial cells from heart tissue of Tek-CreERT: R26R tdTomato mice after sham injury were collected and served as native coronary endothelial cells. ( a ) Principal component analysis clustering show MEndoT-derived cells are a subset cell population with characteristics that were closer to native endothelial cells than native fibroblasts. ( b ) p53 is specifically and significantly upregulated in MEndoT-derived cells. Heatmap show significantly expressed genes indicative of ( c ) fibroblast lineage commitment and ( d ) endothelial lineage commitment (all genes in b-d have a q-value

    Article Snippet: Immunofluorescent staining of frozen sections (7 µm) was performed using primary antibodies to vascular endothelial cadherin (VECAD, ab33168), CD31 (ab28364), von Willebrand factor (vWF, ab11713), endothelial nitric oxide synthase (eNOS, ab5589), occludin (ab31721, all from Abcam, Cambridge, UK), Tek (AF762, R & D Systems, Minnesota, MN, USA), isolectin B4 (B-1205, Vector Labs, Burlingame, CA, USA), p53 (ab31333, Abcam), and associated fluorescein-conjugated secondary antibodies following the manufacturer instructions.

    Techniques: RNA Sequencing Assay, Derivative Assay, Isolation, Mouse Assay, Labeling, Flow Cytometry

    Expression of endothelial markers in mesenchymal-endothelial transition (MEndoT)-derived cells in the heart tissue of Col1a2-CreERT: R26R tdTomato mice after cardiac hypertrophy. ( a-d ) Immunofluorescence staining for endothelial cell markers in heart tissue of Col1a2-CreERT: R26R tdTomato mice after transverse aortic constriction (TAC). ( a ) VECAD expression and the percentage of tdTomato labeled cells expressing VECAD. ( b ) Tek expression and the percentage of tdTomato labeled cells expressing Tek. ( c ) Isolectin B4 expression and the percentage of tdTomato labeled cells expressing isolectin B4. ( d ) CD31 expression and the percentage of tdTomato labeled cells expressing CD31. ( e ) Flow cytometry of isolectin B4 14 days post sham or TAC. (All graphs show mean ± S.E.M; n = 3 animals/group, * p

    Journal: Scientific Reports

    Article Title: Mesenchymal-endothelial transition-derived cells as a potential new regulatory target for cardiac hypertrophy

    doi: 10.1038/s41598-020-63671-8

    Figure Lengend Snippet: Expression of endothelial markers in mesenchymal-endothelial transition (MEndoT)-derived cells in the heart tissue of Col1a2-CreERT: R26R tdTomato mice after cardiac hypertrophy. ( a-d ) Immunofluorescence staining for endothelial cell markers in heart tissue of Col1a2-CreERT: R26R tdTomato mice after transverse aortic constriction (TAC). ( a ) VECAD expression and the percentage of tdTomato labeled cells expressing VECAD. ( b ) Tek expression and the percentage of tdTomato labeled cells expressing Tek. ( c ) Isolectin B4 expression and the percentage of tdTomato labeled cells expressing isolectin B4. ( d ) CD31 expression and the percentage of tdTomato labeled cells expressing CD31. ( e ) Flow cytometry of isolectin B4 14 days post sham or TAC. (All graphs show mean ± S.E.M; n = 3 animals/group, * p

    Article Snippet: Immunofluorescent staining of frozen sections (7 µm) was performed using primary antibodies to vascular endothelial cadherin (VECAD, ab33168), CD31 (ab28364), von Willebrand factor (vWF, ab11713), endothelial nitric oxide synthase (eNOS, ab5589), occludin (ab31721, all from Abcam, Cambridge, UK), Tek (AF762, R & D Systems, Minnesota, MN, USA), isolectin B4 (B-1205, Vector Labs, Burlingame, CA, USA), p53 (ab31333, Abcam), and associated fluorescein-conjugated secondary antibodies following the manufacturer instructions.

    Techniques: Expressing, Derivative Assay, Mouse Assay, Immunofluorescence, Staining, Labeling, Flow Cytometry