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E2F1 antibody (E2F Transcription Factor 1) (pHis357)

Details for Product anti-E2F1 Antibody No. ABIN650836, Supplier: Log in to see
Antigen
  • CG6376
  • DRTF1/E2F
  • DmE2F-1
  • Dmel\\CG6376
  • Dp
  • E(Sev-CycE)3A
  • E(var)3-93E
  • E(var)3-95E
  • E(var)93E
  • E2F
  • E2F-1
  • E2F1
  • E2f1
  • Evar(3)164
  • dE2F
  • dE2F1
  • dE2f
  • dE2f1
  • de2f1
  • def21
  • drosE2F1
  • e2f
  • e2f1
  • l(3)07172
  • l(3)j3B1
  • l(3)j3C2
  • l(3)rM729
  • RBAP1
  • RBBP3
  • RBP3
  • mKIAA4009
  • xE2F
  • ATE2FB
  • E2F TRANSCRIPTION FACTOR-1 E2F1
  • E2F transcription factor 1
  • E2FB
  • E2FB TRANSCRIPTION FACTOR
Alternatives
anti-Human E2F1 antibody for Immunofluorescence
Epitope
pHis357
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Reactivity
Human
335
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Host
Rabbit
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Clonality (Clone)
Polyclonal ()
Conjugate
This E2F1 antibody is un-conjugated
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Application
Dot Blot (DB)
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Supplier
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Immunogen This E2F1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding H357 of human E2F1.
Clone RB07916
Isotype Ig
Specificity This Phospho-E2F1-H357 antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding H357 of human E2F1.
Purification This antibody is purified through a protein A column, followed by peptide affinity purification.
Alternative Name E2F1 (E2F1 Antibody Abstract)
Background The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis.
Synonyms: Retinoblastoma-associated protein 1, RBAP-1, PBR3, PRB-binding protein E2F-1, Retinoblastoma-binding protein 3, RBBP-3, Transcription factor E2F1, E2F-1,RBBP3, E2F1
Molecular Weight 46920 DA
Gene ID 1869
UniProt Q01094
Research Area Transcription Factors, Phospho-specific antibodies, Signaling
Pathways p53 Signaling, Cell Division Cycle
Application Notes DB = 1:500
Restrictions For Research Use only
Format Liquid
Concentration 0.26 mg/mL
Buffer PBS with 0.09 % (W/V) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Expiry Date 6 months
Supplier Images
Dot Blot (DB) image for anti-E2F1 antibody (E2F Transcription Factor 1) (pHis357) (ABIN650836) Dot blot analysis of Phospho-hE2F1-H357 Pab (ABIN650836) on nitrocellulose membrane. ...
Background publications Paik, Wang, Liu et al.: "Regulation of E2F1-induced apoptosis by the nucleolar protein RRP1B." in: The Journal of biological chemistry, Vol. 285, Issue 9, pp. 6348-63, 2010 (PubMed).

Pulikkan, Dengler, Peramangalam et al.: "Cell-cycle regulator E2F1 and microRNA-223 comprise an autoregulatory negative feedback loop in acute myeloid leukemia." in: Blood, Vol. 115, Issue 9, pp. 1768-78, 2010 (PubMed).

Yang, Feng, Jiang et al.: "miR-449a and miR-449b are direct transcriptional targets of E2F1 and negatively regulate pRb-E2F1 activity through a feedback loop by targeting CDK6 and CDC25A." in: Genes & development, Vol. 23, Issue 20, pp. 2388-93, 2009 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).