Anti-TRF1 (phospho S219)抗体(ab79187)


  • 产品名称Anti-TRF1 (phospho S219)抗体
    参阅全部 TRF1 一抗
  • 描述
    兔多克隆抗体to TRF1 (phospho S219)
  • 经测试应用适用于: WB, ELISAmore details
  • 种属反应性
    与反应: Human
  • 免疫原

    Synthesized phosphopeptide derived from human TRF1 around the phosphorylation site of serine 219 (I-I-SP-Q-K).

  • 阳性对照
    • 293 lysate treated with paclitaxel (1 µM, 24 hours)


  • 形式Liquid
  • 存放说明Frozen Stock (-20C). Shelf life 12 months.
  • 存储溶液Preservative: 0.02% Sodium Azide
    Constituents: 50% Glycerol, PBS (without Mg2+ and Ca2+), 150mM Sodium chloride, pH 7.4
  • Concentration information loading...
  • 纯度Immunogen affinity purified
  • 纯化说明Affinity purified from rabbit antiserum by affinity chromatography using epitope specific phosphopeptide. The antibody against non phosphopeptide was removed by chromatography using non phosphopeptide corresponding to the phosphorylation site.
  • 克隆多克隆
  • 同种型IgG
  • 研究领域


Our Abpromise guarantee covers the use of ab79187 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

应用 Ab评论 说明
WB 1/500 - 1/1000. Predicted molecular weight: 50 kDa.
ELISA 1/40000.


  • 功能Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.
  • 组织特异性Highly expressed and ubiquitous. Isoform Pin2 predominates.
  • 序列相似性Contains 1 HTH myb-type DNA-binding domain.
  • 结构域The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules.
    The TRFH dimerization region mediates the interaction with TINF2.
  • 翻译后修饰Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.
    ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
    Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome.
  • 细胞定位Nucleus. Cytoplasm > cytoskeleton > spindle. Chromosome > telomere. Colocalizes with telomeric DNA in interphase and metaphase cells and is located at chromosome ends during metaphase. Associates with the mitotic spindle.
  • Information by UniProt
  • 数据库链接
  • 别名
    • hTRF1 AS antibody
    • NIMA interacting protein 2 antibody
    • NIMA-interacting protein 2 antibody
    • PIN 2 antibody
    • PIN2 antibody
    • t TRF1 antibody
    • Telomeric protein Pin2 antibody
    • Telomeric protein Pin2/TRF1 antibody
    • Telomeric repeat binding factor (NIMA interacting) 1 antibody
    • Telomeric repeat binding factor 1 antibody
    • Telomeric repeat binding protein 1 antibody
    • Telomeric repeat-binding factor 1 antibody
    • TERF 1 antibody
    • Terf1 antibody
    • TERF1_HUMAN antibody
    • TRBF 1 antibody
    • TRBF1 antibody
    • TRF 1 antibody
    • TRF antibody
    • TTAGGG repeat binding factor 1 antibody
    • TTAGGG repeat-binding factor 1 antibody
    see all

Anti-TRF1 (phospho S219) antibody 图像

  • Lanes 1 - 2 : Anti-TRF1 (phospho S219) antibody (ab79187) at 1/500 dilution
    Lane 3 : A different TRF1 antibody (ab63374)

    Lane 1 : 293 cells treated with paclitaxel (1 µM, 24 hours)
    Lane 2 : 293 cells treated with paclitaxel (1 µM, 24 hours) with immunizing phosphopeptide at 10 µg
    Lane 3 : 293 cells treated with paclitaxel (1 µM, 24 hours)

    Lysates/proteins at 30 µg per lane.

    Predicted band size : 50 kDa
    Observed band size : 50 kDa

Anti-TRF1 (phospho S219) antibody (ab79187)参考文献

ab79187 has not yet been referenced specifically in any publications.

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