nanog  (ABclonal)

 
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  • 91
    Name:
    NANOG Antibody
    Description:
    Polyclonal
    Catalog Number:
    a14150
    Modification:
    Polyclonal
    Price:
    [130.0, 220.0, 380.0]
    Applications:
    Western Blot
    Host:
    Rabbit
    Size:
    50 ul 100 ul 200 ul
    Category:
    Antibody
    Antibody Type:
    Primary antibody
    Reactivity:
    Human Mouse Rat
    Buy from Supplier


    Structured Review

    ABclonal nanog
    Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and <t>Nanog</t> and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as <t>BRD4</t> or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).
    Polyclonal
    https://www.bioz.com/result/nanog/product/ABclonal
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nanog - by Bioz Stars, 2020-07
    91/100 stars

    Images

    1) Product Images from "Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription"

    Article Title: Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription

    Journal: Cell Research

    doi: 10.1038/cr.2017.68

    Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and Nanog and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as BRD4 or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).
    Figure Legend Snippet: Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and Nanog and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as BRD4 or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).

    Techniques Used: Western Blot, Expressing, Cell Culture, Quantitative RT-PCR, Marker, Activation Assay

    Related Articles

    other:

    Article Title: Anti-tumor Activity of Bufalin by Inhibiting c-MET Mediated MEK/ERK and PI3K/AKT Signaling Pathways in Gallbladder Cancer
    Article Snippet: Primary antibodies include anti-Bcl-2, anti-Mcl-1, anti-Bax, anti-P21, anti-P27, anti-MMP9 and anti-MMP2 antibodies were purchased from Abcam; anti-E-cadherin, anti-Snail, anti-CD44, anti-CD133, anti-Sox2, anti-Oct4 and anti-Nanog antibodies were purchased from ABclonal; anti-AKT, anti-p-AKT, anti-p-ERK, anti- MEK, anti-p-MEK, anti-p-P38, anti-P38, anti-p-JNK and anti-JNK antibodies were purchased from CST.

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  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
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  • Contact
  • Bioz Stars
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  • 91
    ABclonal nanog
    Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and <t>Nanog</t> and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as <t>BRD4</t> or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).
    Nanog, supplied by ABclonal, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanog/product/ABclonal
    Average 91 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    nanog - by Bioz Stars, 2020-07
    91/100 stars
      Buy from Supplier

    Image Search Results


    Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and Nanog and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as BRD4 or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).

    Journal: Cell Research

    Article Title: Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription

    doi: 10.1038/cr.2017.68

    Figure Lengend Snippet: Histone crotonylation is enriched in and required for self-renewal of mESCs. (A) WB analysis showing a significantly higher level of histone crotonylation in mESC than in differentiated embryoid bodies (EB). CGR8 mESC were induced to differentiate by suspension culture in dish for 9 days. (B) WB analysis showing induced expression of WT HDAC1 and HDAC1-VRPP in CGR8 cells. HA antibody detected only Dox-induced HA-tagged HDAC1 or HDAC1-VRPP, whereas HDAC1 antibody detected both induced and endogenous HDAC1 proteins. (C) Contrast-phase images of control, WT HDAC1 and HDAC1-VRPP CGR8 colonies cultured for 9 days with or without Dox. (D) WB analysis showing the effect of induced expression of WT HDAC1 and HDAC1-VRPP on the levels of mESC core transcription factors Sox2, Oct4 and Nanog and histone crotonylation and histone acetylation. Note that reduced levels of Sox2, Oct4, Nanog, histone crotonylation and histone acetylation were observed upon 3 days of Dox treatment. (E) Confirmation of induced differentiation upon Dox-induced expression of WT HDAC1 or HDAC1-VRPP by qRT-PCR analysis of indicated differentiation marker genes. (F) Working model illustrating a non-redundant function of histone crotonylation to histone acetylation in transcription. CBP/p300 and MOF catalyze both histone acetylation and crotonylation, which in turn recruit corresponding reader proteins such as BRD4 or DPF2 and AF9, and facilitate transcriptional activation (left panel). Selective decrotonylation by HDCR1-VRPP is sufficient to repress transcription, indicating that histone crotonylation is required for transcriptional activation (right panel).

    Article Snippet: The following antibodies were used in this study: pan-Kac (PTM-Biolabs 101), pan-Kcr (PTM-Biolabs 501), H3K4cr (PTM-Biolabs PTM-527), H3K9cr (PTM-Biolabs 516), H3K18cr (PTM-Biolabs 517), H3K23cr (PTM-Biolabs 519), H4K8cr (PTM-Biolabs 522), H4K12cr (PTM-Biolabs 523), H4ac (Millipore 05-1355), H3 (Epitomics M1309-1), Flag (Sigma 7425/1804), HA (Santa Cruz SC-805), Gal4DBD (Santa Cruz SC-510), GAPDH (Abmart ), actin (Huabio M1210-2), HDAC1 (ABclonal A0238), HDAC2 (ABclonal A2084) and HDAC3 (ABclonal A2139), BRD4 (Abcam ab128874), Sox2 (Abcam ab92494), Oct4 (Santa Cruz sc-5279) and Nanog (Abclonal A3232).

    Techniques: Western Blot, Expressing, Cell Culture, Quantitative RT-PCR, Marker, Activation Assay

    Bufalin hindered the development of gallbladder cancer stem cells. ( A, B ) Western blot analyzed the expression of stemness-associated surface proteins, CD133 and CD44 after 48 hours of treatment by Bufalin at different concentrations (0, 50, 100 nM, respectively). ( C ) Low attachment sphere-forming assay detected the cell sphere size after 48 hours of treatment by Bufalin. ( D, E ) Western blot analyzed the expression of stemness-associated proteins, Sox2, Oct4 and Nanog after 48 hours of treatment by Bufalin at different concentrations (0, 50, 100 nM, respectively). ( F, G ) Low attachment sphere-forming assay detected the cell sphere number of Bufalin on 5-FU resistant GBC-SD cells. (* P

    Journal: Journal of Cancer

    Article Title: Anti-tumor Activity of Bufalin by Inhibiting c-MET Mediated MEK/ERK and PI3K/AKT Signaling Pathways in Gallbladder Cancer

    doi: 10.7150/jca.38393

    Figure Lengend Snippet: Bufalin hindered the development of gallbladder cancer stem cells. ( A, B ) Western blot analyzed the expression of stemness-associated surface proteins, CD133 and CD44 after 48 hours of treatment by Bufalin at different concentrations (0, 50, 100 nM, respectively). ( C ) Low attachment sphere-forming assay detected the cell sphere size after 48 hours of treatment by Bufalin. ( D, E ) Western blot analyzed the expression of stemness-associated proteins, Sox2, Oct4 and Nanog after 48 hours of treatment by Bufalin at different concentrations (0, 50, 100 nM, respectively). ( F, G ) Low attachment sphere-forming assay detected the cell sphere number of Bufalin on 5-FU resistant GBC-SD cells. (* P

    Article Snippet: Primary antibodies include anti-Bcl-2, anti-Mcl-1, anti-Bax, anti-P21, anti-P27, anti-MMP9 and anti-MMP2 antibodies were purchased from Abcam; anti-E-cadherin, anti-Snail, anti-CD44, anti-CD133, anti-Sox2, anti-Oct4 and anti-Nanog antibodies were purchased from ABclonal; anti-AKT, anti-p-AKT, anti-p-ERK, anti- MEK, anti-p-MEK, anti-p-P38, anti-P38, anti-p-JNK and anti-JNK antibodies were purchased from CST.

    Techniques: Western Blot, Expressing