E2F2 Antibody Blocking Peptide(bs-1001P)-500ug

E2F2 Antibody Blocking Peptide

(bs-1001P)-500ug
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  • ¥880
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  • bs-1001P
  • 2025年10月16日
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      500ug

    产品编号bs-1001P
    英文名称E2F2 Antibody Blocking Peptide
    中文名称转录因子E2F-2封闭多肽
    英文别名dE2F2; E2F-2; E2F2; E2F2_HUMAN; Transcription factor E2F2; E2F transcription factor 2.
    性状Lyophilized
    纯化方法HPLC
    研究领域

    Epigenetics and Nuclear Signaling > Transcription > Domain Families > Forkhead Box

    Epigenetics and Nuclear Signaling > Transcription > Other factors

    Epigenetics and Nuclear Signaling > Transcription > Transcription Factors

    亚基Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F2 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB1, thus releasing the active complex. Binds EAPP.
    亚细胞定位Nucleus.
    组织特异性Highest level of expression is found in placenta, low levels are found in lung. Found as well in many immortalized cell lines derived from tumor samples.
    翻译后修饰Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase (By similarity).
    相似性Belongs to the E2F/DP family.
    功能Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    背景资料E2F/DP family winged-helix DNA-binding domain. This family contains the transcription factor E2F and its dimerisation partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.

     

     

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