histone h4 polyclonal antibody  (Abcam)

 
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    Name:
    Anti Histone H4 antibody
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    Catalog Number:
    ab134212
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    Structured Review

    Abcam histone h4 polyclonal antibody

    https://www.bioz.com/result/histone h4 polyclonal antibody/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    histone h4 polyclonal antibody - by Bioz Stars, 2020-09
    99/100 stars

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    Related Articles

    Immunohistochemistry:

    Article Title: Analysis of the Staphylococcus aureus abscess proteome identifies antimicrobial host proteins and bacterial stress responses at the host-pathogen interface
    Article Snippet: .. Additional unstained tissue sections were deparaffinized and processed for immunohistochemistry with rabbit polyclonal anti-sera against myeloperoxidase (MPO-7, Dako) and histone H4 (ab61255, Abcam). ..

    other:

    Article Title: Histone H4 expression is cooperatively maintained by IKKβ and Akt1 which attenuates cisplatin-induced apoptosis through the DNA-PK/RIP1/IAPs signaling cascade
    Article Snippet: Reagents Anti-phospho-DNA-PKcs and -histone H4 antibodies were from Abcam (Cambridge, MA, UN).

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  • 99
    Abcam anti h3 antibody
    Commercial H3 K122Ac antibodies are not specific. a Wing and eye imaginal discs with GFP-negative mutant clones. Merged images show the nuclear marker DAPI in blue , H3 K122Ac in magenta , and GFP + and GFP − regions demarcate histone wild-type cells and histone mutant cells, respectively. Grayscale images are the individual H3 K122Ac channels. b Western blot analysis with the Abcam <t>anti-H3</t> K122Ac antibody using acid-extracted histones collected from HEK293T cells transiently transfected with YFP-tagged WT or mutant histone H3 expression plasmid (H3.1 K115R, K122R, T118E, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified H3 and/or other modification(s) besides H3 K122Ac. c Immunoprecipitation (IP) analysis with the Abcam anti-H3 K122Ac antibody using nuclear extract from stable cell lines expressing Flag-tagged WT or mutant histone H3 (H3.1 K115R, K122R, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified histone H3 and/or other modification(s) besides H3 K122Ac
    Anti H3 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti h3 antibody/product/Abcam
    Average 99 stars, based on 43 article reviews
    Price from $9.99 to $1999.99
    anti h3 antibody - by Bioz Stars, 2020-09
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    hh3  (Abcam)
    89
    Abcam hh3
    NFAT4 Is Rephosphorylated within the Nucleus Considerably More Quickly Than NFAT1 (A) Images compare nuclear export of NFAT4-GFP between a control cell and one exposed to leptomycin B (LMB; 100 nM). Nuclear export was initiated by removal of external Ca 2+ in the presence of cyclosporine A. (B) Aggregate data from several experiments are compared. (C) Western blot shows gel shift of NFAT4-GFP from nuclear extract after stimulation and then at different times (2–20 min) after initiation of export (see bottom of G for timings). (D) Graph plots relative gel shift as a function of time up to 20 min after the initiation of nuclear export. A decreased gel shift denotes rephosphorylation. (E) Gel shift for nuclear NFAT1-GFP under conditions identical to (C). (F) Graph shows relative gel shift for NFAT1-GFP, as in (D). (G) Gel shift for the SP3NFAT1-NFAT4-GFP construct. (H) Graph plots relative gel shift for SP3NFAT1-NFAT4-GFP, as in (D). For the gels in (C), (E), and (G), conditions for each lane are shown only in (G). For the resting condition (indicated as Rest), no detectable NFAT was seen in any of the gels because the gels show nuclear extract and, at rest, there is very little NFAT in the nucleus. (I) Blot compares kinetics of phosphorylation of serine 165 in NFAT4 from the nuclear fraction, denoted as P-S165. (J) As in (I), but phosphorylation of serine 177 (P-S177) in NFAT1 was measured. (K) Graphs plot the kinetics of phosphorylation of serine 165 NFAT4 and SP3N1-N4 or serine 177 in NFAT1. In (C), (E), (G), (I), and (J), <t>HH3</t> (histone H3) was used as a nuclear marker and ERK was taken as a cytoplasmic marker. Rest denotes the non-stimulated state. Thap + LMB represents the gel shift seen 40 min after stimulation with thapsigargin in the presence of LMB and external Ca 2+ , when NFAT had fully accumulated in the nucleus. Nuclear extract was isolated at the different times indicated. In all panels, 100 nM leptomycin B was added 10 min before thapsigargin and then maintained throughout. In the graphs, data are represented as mean ± SEM. See also Figure S5 .
    Hh3, supplied by Abcam, used in various techniques. Bioz Stars score: 89/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hh3/product/Abcam
    Average 89 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    hh3 - by Bioz Stars, 2020-09
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    91
    Abcam antibodies against th2b
    Detection of <t>TH2B</t> protein using Western blotting and regression models showing variation in the intensity of TH2B in sperm as related to fertility scores in Holstein bulls. a MM stands for molecular markers; LF1–5 and HF1–5 refer to samples from low vs. high fertility bulls, respectively. The same amounts of nuclear proteins were loaded into each lane. As TH2B is a nuclear protein and the expression levels of our internal control (Lamin B1) were not stable, another protein band (~25 KDa) served as the internal control. b The regression line was determined using the model predicted intensity values for each fertility score using the mixed effects model. A scatter plot of unadjusted data points was superimposed on the regression line plot. Regression equations are shown for high fertility ( y = −22,315 × + 89,049) and low fertility ( y = 9603 × + 50,993) bulls
    Antibodies Against Th2b, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against th2b/product/Abcam
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibodies against th2b - by Bioz Stars, 2020-09
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    89
    Abcam acetyllysine
    A SUMOylation/acetylation switch at K13 controls ΔLf transcriptional activity. (A) K13 is the main acetylation site. Cells were co-transfected by WT, the mutant constructs or the null vector and then lysed 24 h later. Lysates were immunoprecipitated with <t>anti-acetyllysine</t> antibodies and immunoblotted with M2. Input was immunoblotted with either M2 or anti-GAPDH antibodies and used as loading control (n = 3). B) Relative transcriptional activity of K13 and K379 mutants compared to WT. Cells were co-transfected with pGL3-S1 Skp1 -Luc reporter vector and WT, K13 or K379. His-SUMO-1 expression vector and/or the deacetylase inhibitor Trichostatin A (TSA, 15 ng/mL) were used to modulate the acetylation/SUMOylation ratio. Relative luciferase activities are expressed as described in Materials and Methods (n≥3; p
    Acetyllysine, supplied by Abcam, used in various techniques. Bioz Stars score: 89/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/acetyllysine/product/Abcam
    Average 89 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Commercial H3 K122Ac antibodies are not specific. a Wing and eye imaginal discs with GFP-negative mutant clones. Merged images show the nuclear marker DAPI in blue , H3 K122Ac in magenta , and GFP + and GFP − regions demarcate histone wild-type cells and histone mutant cells, respectively. Grayscale images are the individual H3 K122Ac channels. b Western blot analysis with the Abcam anti-H3 K122Ac antibody using acid-extracted histones collected from HEK293T cells transiently transfected with YFP-tagged WT or mutant histone H3 expression plasmid (H3.1 K115R, K122R, T118E, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified H3 and/or other modification(s) besides H3 K122Ac. c Immunoprecipitation (IP) analysis with the Abcam anti-H3 K122Ac antibody using nuclear extract from stable cell lines expressing Flag-tagged WT or mutant histone H3 (H3.1 K115R, K122R, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified histone H3 and/or other modification(s) besides H3 K122Ac

    Journal: Epigenetics & Chromatin

    Article Title: Mutations that prevent or mimic persistent post-translational modifications of the histone H3 globular domain cause lethality and growth defects in Drosophila

    doi: 10.1186/s13072-016-0059-3

    Figure Lengend Snippet: Commercial H3 K122Ac antibodies are not specific. a Wing and eye imaginal discs with GFP-negative mutant clones. Merged images show the nuclear marker DAPI in blue , H3 K122Ac in magenta , and GFP + and GFP − regions demarcate histone wild-type cells and histone mutant cells, respectively. Grayscale images are the individual H3 K122Ac channels. b Western blot analysis with the Abcam anti-H3 K122Ac antibody using acid-extracted histones collected from HEK293T cells transiently transfected with YFP-tagged WT or mutant histone H3 expression plasmid (H3.1 K115R, K122R, T118E, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified H3 and/or other modification(s) besides H3 K122Ac. c Immunoprecipitation (IP) analysis with the Abcam anti-H3 K122Ac antibody using nuclear extract from stable cell lines expressing Flag-tagged WT or mutant histone H3 (H3.1 K115R, K122R, or K115R/K122R) shows that the anti-H3 K122Ac antibody non-specifically recognizes unmodified histone H3 and/or other modification(s) besides H3 K122Ac

    Article Snippet: The eluted supernatants were separated by SDS-PAGE, probed with the anti-H3 antibody (Rabbit pAb: Abcam 1791) and anti-Flag antibody (Mouse mAb: Sigma 3165).

    Techniques: Mutagenesis, Clone Assay, Marker, Western Blot, Transfection, Expressing, Plasmid Preparation, Modification, Immunoprecipitation, Stable Transfection

    NFAT4 Is Rephosphorylated within the Nucleus Considerably More Quickly Than NFAT1 (A) Images compare nuclear export of NFAT4-GFP between a control cell and one exposed to leptomycin B (LMB; 100 nM). Nuclear export was initiated by removal of external Ca 2+ in the presence of cyclosporine A. (B) Aggregate data from several experiments are compared. (C) Western blot shows gel shift of NFAT4-GFP from nuclear extract after stimulation and then at different times (2–20 min) after initiation of export (see bottom of G for timings). (D) Graph plots relative gel shift as a function of time up to 20 min after the initiation of nuclear export. A decreased gel shift denotes rephosphorylation. (E) Gel shift for nuclear NFAT1-GFP under conditions identical to (C). (F) Graph shows relative gel shift for NFAT1-GFP, as in (D). (G) Gel shift for the SP3NFAT1-NFAT4-GFP construct. (H) Graph plots relative gel shift for SP3NFAT1-NFAT4-GFP, as in (D). For the gels in (C), (E), and (G), conditions for each lane are shown only in (G). For the resting condition (indicated as Rest), no detectable NFAT was seen in any of the gels because the gels show nuclear extract and, at rest, there is very little NFAT in the nucleus. (I) Blot compares kinetics of phosphorylation of serine 165 in NFAT4 from the nuclear fraction, denoted as P-S165. (J) As in (I), but phosphorylation of serine 177 (P-S177) in NFAT1 was measured. (K) Graphs plot the kinetics of phosphorylation of serine 165 NFAT4 and SP3N1-N4 or serine 177 in NFAT1. In (C), (E), (G), (I), and (J), HH3 (histone H3) was used as a nuclear marker and ERK was taken as a cytoplasmic marker. Rest denotes the non-stimulated state. Thap + LMB represents the gel shift seen 40 min after stimulation with thapsigargin in the presence of LMB and external Ca 2+ , when NFAT had fully accumulated in the nucleus. Nuclear extract was isolated at the different times indicated. In all panels, 100 nM leptomycin B was added 10 min before thapsigargin and then maintained throughout. In the graphs, data are represented as mean ± SEM. See also Figure S5 .

    Journal: Molecular Cell

    Article Title: Control of NFAT Isoform Activation and NFAT-Dependent Gene Expression through Two Coincident and Spatially Segregated Intracellular Ca2+ Signals

    doi: 10.1016/j.molcel.2016.11.011

    Figure Lengend Snippet: NFAT4 Is Rephosphorylated within the Nucleus Considerably More Quickly Than NFAT1 (A) Images compare nuclear export of NFAT4-GFP between a control cell and one exposed to leptomycin B (LMB; 100 nM). Nuclear export was initiated by removal of external Ca 2+ in the presence of cyclosporine A. (B) Aggregate data from several experiments are compared. (C) Western blot shows gel shift of NFAT4-GFP from nuclear extract after stimulation and then at different times (2–20 min) after initiation of export (see bottom of G for timings). (D) Graph plots relative gel shift as a function of time up to 20 min after the initiation of nuclear export. A decreased gel shift denotes rephosphorylation. (E) Gel shift for nuclear NFAT1-GFP under conditions identical to (C). (F) Graph shows relative gel shift for NFAT1-GFP, as in (D). (G) Gel shift for the SP3NFAT1-NFAT4-GFP construct. (H) Graph plots relative gel shift for SP3NFAT1-NFAT4-GFP, as in (D). For the gels in (C), (E), and (G), conditions for each lane are shown only in (G). For the resting condition (indicated as Rest), no detectable NFAT was seen in any of the gels because the gels show nuclear extract and, at rest, there is very little NFAT in the nucleus. (I) Blot compares kinetics of phosphorylation of serine 165 in NFAT4 from the nuclear fraction, denoted as P-S165. (J) As in (I), but phosphorylation of serine 177 (P-S177) in NFAT1 was measured. (K) Graphs plot the kinetics of phosphorylation of serine 165 NFAT4 and SP3N1-N4 or serine 177 in NFAT1. In (C), (E), (G), (I), and (J), HH3 (histone H3) was used as a nuclear marker and ERK was taken as a cytoplasmic marker. Rest denotes the non-stimulated state. Thap + LMB represents the gel shift seen 40 min after stimulation with thapsigargin in the presence of LMB and external Ca 2+ , when NFAT had fully accumulated in the nucleus. Nuclear extract was isolated at the different times indicated. In all panels, 100 nM leptomycin B was added 10 min before thapsigargin and then maintained throughout. In the graphs, data are represented as mean ± SEM. See also Figure S5 .

    Article Snippet: Antibodies against ERK (1:5,000, rabbit polyclonal; Santa Cruz Biotechnology), GFP (1:2,000, rabbit polyclonal; Cell Signaling), HH3 (Histone H3; 1:5,000, rabbit polyclonal; Abcam), InsP3 type I receptor (1:1,000, mouse monoclonal; Abcam), anti-phospho Ser177 NFAT1 (Santa Cruz; 1:2,000 dilution), anti-phospho Ser165 NFAT4 (Abcam; 1:2,000), and IL-5 (Santa Cruz; 1:500) were used.

    Techniques: Western Blot, Electrophoretic Mobility Shift Assay, Construct, Marker, Isolation

    Detection of TH2B protein using Western blotting and regression models showing variation in the intensity of TH2B in sperm as related to fertility scores in Holstein bulls. a MM stands for molecular markers; LF1–5 and HF1–5 refer to samples from low vs. high fertility bulls, respectively. The same amounts of nuclear proteins were loaded into each lane. As TH2B is a nuclear protein and the expression levels of our internal control (Lamin B1) were not stable, another protein band (~25 KDa) served as the internal control. b The regression line was determined using the model predicted intensity values for each fertility score using the mixed effects model. A scatter plot of unadjusted data points was superimposed on the regression line plot. Regression equations are shown for high fertility ( y = −22,315 × + 89,049) and low fertility ( y = 9603 × + 50,993) bulls

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Detection of TH2B protein using Western blotting and regression models showing variation in the intensity of TH2B in sperm as related to fertility scores in Holstein bulls. a MM stands for molecular markers; LF1–5 and HF1–5 refer to samples from low vs. high fertility bulls, respectively. The same amounts of nuclear proteins were loaded into each lane. As TH2B is a nuclear protein and the expression levels of our internal control (Lamin B1) were not stable, another protein band (~25 KDa) served as the internal control. b The regression line was determined using the model predicted intensity values for each fertility score using the mixed effects model. A scatter plot of unadjusted data points was superimposed on the regression line plot. Regression equations are shown for high fertility ( y = −22,315 × + 89,049) and low fertility ( y = 9603 × + 50,993) bulls

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Western Blot, Expressing

    The interactome of TH2B protein with chromatin remodeling proteins. Cytoscape was used in conjunction with large protein- protein databases, understanding protein-DNA and genetic interactions. The circles represent the genes, links represent the interactions, edges depict protein-protein interactions. The bigger circle indicates the significance of expression of that gene for the given process involved. The colors represent the involvement in same function or process

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: The interactome of TH2B protein with chromatin remodeling proteins. Cytoscape was used in conjunction with large protein- protein databases, understanding protein-DNA and genetic interactions. The circles represent the genes, links represent the interactions, edges depict protein-protein interactions. The bigger circle indicates the significance of expression of that gene for the given process involved. The colors represent the involvement in same function or process

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Expressing

    Threshold dotplot of TH2B and H2B between bovine and human. The emboss dotmatcher of predicted TH2B of bull vs. TH2B of human is a perfect diagonal line with two frame shift mutation sites ( a ). The emboss dotmatcher of H2B of bull vs. H2B of human revealed a low complexity region between bovine H2B and human H2B ( b ). Dotmatcher of TH2B of bull vs. H2B of bull showed two areas of different amino acids ( c )

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Threshold dotplot of TH2B and H2B between bovine and human. The emboss dotmatcher of predicted TH2B of bull vs. TH2B of human is a perfect diagonal line with two frame shift mutation sites ( a ). The emboss dotmatcher of H2B of bull vs. H2B of human revealed a low complexity region between bovine H2B and human H2B ( b ). Dotmatcher of TH2B of bull vs. H2B of bull showed two areas of different amino acids ( c )

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Mutagenesis

    Protein-protein interactions involving TH2B. TH2B/H1FNT involved in replacement of TNPs by protamines in human and mouse are depicted in ( a ; b ) and the missing link with possibly same role in bovines ( c )

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Protein-protein interactions involving TH2B. TH2B/H1FNT involved in replacement of TNPs by protamines in human and mouse are depicted in ( a ; b ) and the missing link with possibly same role in bovines ( c )

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques:

    Differential expression of TH2B in sperm from bulls with different fertility scores. The negative control showing the absence of TH2B fluorescence in the unstained sperm ( a ). Percentage of sperm expressing TH2B and unstained in high fertility bulls ( b ). The percentage of sperm in low fertility bulls expressing TH2B positive and unstained cells ( c ). The percentage of sperm in FL1-H subset indicates expression of TH2B

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Differential expression of TH2B in sperm from bulls with different fertility scores. The negative control showing the absence of TH2B fluorescence in the unstained sperm ( a ). Percentage of sperm expressing TH2B and unstained in high fertility bulls ( b ). The percentage of sperm in low fertility bulls expressing TH2B positive and unstained cells ( c ). The percentage of sperm in FL1-H subset indicates expression of TH2B

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Expressing, Negative Control, Fluorescence

    Regression models showing in the intensity of TH2B in sperm as related to fertility scores in bulls. The regression line was determined using the model predicted intensity values for each value of fertility score using the mixed effects model. A scatter plot of unadjusted data points was superimposed on the regression line plot. Regression equations are shown for high fertility ( y = −12.3828 × + 56.9464) and low fertility ( y = 2.0450 × + 28.0499) bulls

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Regression models showing in the intensity of TH2B in sperm as related to fertility scores in bulls. The regression line was determined using the model predicted intensity values for each value of fertility score using the mixed effects model. A scatter plot of unadjusted data points was superimposed on the regression line plot. Regression equations are shown for high fertility ( y = −12.3828 × + 56.9464) and low fertility ( y = 2.0450 × + 28.0499) bulls

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques:

    Immunostaining of TH2B in low and high fertility bull spermatozoa. Intensity of TH2B in sperm from low ( a ) and high fertile bulls ( b ) using confocal microscopy. DNA stained with DAPI ( blue ) in a bull sperm; TH2B histone linked to FITC-conjugated secondary antibody ( green ) in bull sperm; merged images of DAPI and FITC; bright field images; and negative controls

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Immunostaining of TH2B in low and high fertility bull spermatozoa. Intensity of TH2B in sperm from low ( a ) and high fertile bulls ( b ) using confocal microscopy. DNA stained with DAPI ( blue ) in a bull sperm; TH2B histone linked to FITC-conjugated secondary antibody ( green ) in bull sperm; merged images of DAPI and FITC; bright field images; and negative controls

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Immunostaining, Confocal Microscopy, Staining

    Cellular localization of TH2B in bull spermatozoa. The intensity of FITC bound to TH2B protein ( a , b and c ). Dominant signal of TH2B coming from sperm head, depict merged images of two sperm using confocal microscope, showing expression dynamics and localization of TH2B in head of bovine spermatozoa ( d )

    Journal: Reproductive Biology and Endocrinology : RB & E

    Article Title: Testis specific histone 2B is associated with sperm chromatin dynamics and bull fertility-a pilot study

    doi: 10.1186/s12958-017-0274-1

    Figure Lengend Snippet: Cellular localization of TH2B in bull spermatozoa. The intensity of FITC bound to TH2B protein ( a , b and c ). Dominant signal of TH2B coming from sperm head, depict merged images of two sperm using confocal microscope, showing expression dynamics and localization of TH2B in head of bovine spermatozoa ( d )

    Article Snippet: Sperm were probed with primary antibodies against TH2B (Rabbit polyclonal to Testes Specific Histone H2B; Abcam, Cambridge, MA, USA; catalog # 23913; 1/200 dilution) at 4 °C overnight followed by a washing step and probing with secondary antibody of donkey anti-rabbit IgG-FITC against TH2B (Santa Cruz, Dallas, Texas, USA; catalog # 2090; 1/5000 dilution) at RT for 1 h, and then with 2.5 mg/ml of DAPI at RT for 10 min. Coverslips were placed onto the slides using a drop of an antifade mounting medium (VECTAshield, H-1000) and sealed using a nail polish border.

    Techniques: Microscopy, Expressing

    A SUMOylation/acetylation switch at K13 controls ΔLf transcriptional activity. (A) K13 is the main acetylation site. Cells were co-transfected by WT, the mutant constructs or the null vector and then lysed 24 h later. Lysates were immunoprecipitated with anti-acetyllysine antibodies and immunoblotted with M2. Input was immunoblotted with either M2 or anti-GAPDH antibodies and used as loading control (n = 3). B) Relative transcriptional activity of K13 and K379 mutants compared to WT. Cells were co-transfected with pGL3-S1 Skp1 -Luc reporter vector and WT, K13 or K379. His-SUMO-1 expression vector and/or the deacetylase inhibitor Trichostatin A (TSA, 15 ng/mL) were used to modulate the acetylation/SUMOylation ratio. Relative luciferase activities are expressed as described in Materials and Methods (n≥3; p

    Journal: PLoS ONE

    Article Title: Modification by SUMOylation Controls Both the Transcriptional Activity and the Stability of Delta-Lactoferrin

    doi: 10.1371/journal.pone.0129965

    Figure Lengend Snippet: A SUMOylation/acetylation switch at K13 controls ΔLf transcriptional activity. (A) K13 is the main acetylation site. Cells were co-transfected by WT, the mutant constructs or the null vector and then lysed 24 h later. Lysates were immunoprecipitated with anti-acetyllysine antibodies and immunoblotted with M2. Input was immunoblotted with either M2 or anti-GAPDH antibodies and used as loading control (n = 3). B) Relative transcriptional activity of K13 and K379 mutants compared to WT. Cells were co-transfected with pGL3-S1 Skp1 -Luc reporter vector and WT, K13 or K379. His-SUMO-1 expression vector and/or the deacetylase inhibitor Trichostatin A (TSA, 15 ng/mL) were used to modulate the acetylation/SUMOylation ratio. Relative luciferase activities are expressed as described in Materials and Methods (n≥3; p

    Article Snippet: Antibodies against the 3xFLAG epitope (mouse monoclonal anti-FLAG M2 antibody, Sigma), HA epitope (mouse monoclonal HA.11 antibody 16B12, Covance Research Products), 6XHis epitope (mouse monoclonal anti-6XHis P5A11 antibody for WB, Biolegend; mouse monoclonal anti-His AD1.10 antibody for IP, Santa Cruz Biotechnology), SUMO-1 (rabbit monoclonal anti-SUMO-1, Millipore), SUMO-2/3 (rabbit polyclonal anti-SUMO-2/3, Millipore), Ubc9 (rabbit monoclonal antibody anti-Ubc9, Cell Signaling), acetyllysine (rabbit polyclonal anti-acetyllysine, ABCAM), GAPDH (rabbit polyclonal anti-glyceraldehyde-3-phosphate dehydrogenase antibody, Santa Cruz Biotechnologies) were used for immunoprecipitation and/or immunoblotting.

    Techniques: Activity Assay, Transfection, Mutagenesis, Construct, Plasmid Preparation, Immunoprecipitation, Expressing, Histone Deacetylase Assay, Luciferase