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Human Polyclonal PA2G4 Primary Antibody for FACS, IHC (p) - ABIN1882075
Zhang, Linn, Liu, Melamed, Tavora, Young, Burger, Hamburger: EBP1, an ErbB3-binding protein, is decreased in prostate cancer and implicated in hormone resistance. in Molecular cancer therapeutics 2008
Targeted profiling of RNA translation reveals mTOR-4EBP1/2-independent translation regulation of mRNAs encoding ribosomal proteins.
In this study, the authors demonstrated that overexpression of ErbB3-binding protein 1 (EBP1) promoted not only a reduction of wild type of p85 subunit of phosphoinositide 3-kinase but also oncogenic mutant forms of p85 which were identified in human cancers.
The results demonstrate an important role of Ebp1 in promoting cell proliferation in Acute Myelogenous Leukemic Cells through the regulation of both rRNA synthesis and Proliferating Cell Nuclear Antigen expression.
results show that EBP1 interacts directly with PPIns and associate with PtdIns(3,4,5)P3 in the nucleolus.
The adapter function of EBP1 P42 stabilized the interaction of FBXW7 with its substrates and promoted FBXW7-mediated degradation of oncogenic targets, enhancing its overall tumor-suppressing function. Results establish distinct physical and functional interactions between FBXW7 and EBP1 isoforms, which yield their mechanistically unique isoform-specific functions of EBP1 in cancer.
The combined determination of Ebp1 and p53 expression levels in cervical cancer patients could support the effective prediction of metastatic potential and patient prognosis.
Data highlight the tissue specificity function of EBP1 isoforms and show that only the oncogene p48 activates MHC II expression in human solid tumors, via STAT1 phosphorylation, in order to affect tumor progression by triggering specific immune response.
Our results suggest a novel function of Ebp1 as a binding protein and negative regulator of Anxa2. The functional association between Anxa2 and EBP1 may participate in regulating cancer cell proliferation and invasion, contributing to cancer progression.
Ebp1 functionality is independent from heat-shock-protein-regulated progression networks in prostate cancer.
P48Ebp1 acts as an oncoprotein.
EBP1 participates in the regulation of intestinal inflammation via mediating Akt signaling pathway.
Data suggest that inhibiting ErbB3-binding protein 1 Ebp1 phosphorylation may be an effective mechanism for inhibiting T-cell activation and proliferation.
Ebp1 p42 isoform regulates the proteasomal degradation of the p85 regulatory subunit of PI3K by recruiting a chaperone-E3 ligase complex HSP70/CHIP.
data suggest that Vpr may inhibit Ebp1 to stabilize p53, which in turn leads to G2 arrest and apoptosis in U87MG cells
identified among endothelial antigens to which antibodies are produced during heart transplant rejection
The major effect of EBP1 on ErbB2 mRNA expression levels is at the transcriptional level.
Down-regulation of the ErbB3 binding protein 1 in human bladder cancer promotes tumor progression and cell proliferation.
Performed immunohistochemical analysis on 132 primary adenoid cystic carcinoma and adjacent non-cancerous tissues.The expression of EBP1 was significantly higher in non-cancerous adjacent tissues compared with corresponding cancer tissues.
It was shown that high level of Ebp1 expression led to enhancee HDM2 phosphorylation by Akt and inhibited the self-ubiquitination of HDM2 by up-regulation of Akt activity.
the Ebp1 promoter localizes between -664 nt and the initiation site of the Ebp1 gene, +317-nt long sequence in the noncoding region is required for regulation of Ebp1 gene expression.
these findings establish an interaction between Pa2G4 and Six1, and demonstrate that it has an important role in the development of tissues affected in Branchiootorenal Spectrum disorder.
These results strongly suggest that PA2G4 may have an important role on the regulation of DNA replication in eukaryotic cells.
identifies EBP1 as a novel pluripotency cofactor and provides insight into potential mechanisms used by DPPA4 in regulating pluripotency through its association with EBP1
EBP1 is a novel component of the ZFP809-TRIM28 silencing complex to restrict the moloney murine leukemia virus replication in embryonic cells.
Ebp1 has a role in the regulation of embryonic muscle progenitors and adult muscle stem cells, which likely operates independently of ErbB3 signaling
EBP1 is in the cytoplasm & nucleolus. Nucleolar localization requires AA sequences at the NH2- and COOH-ends. Overexpression inhibits proliferation of human fibroblasts. It is part of RNP complexes & associates with different rRNAs.
IGF-1 production and IGBP-3 and 4 protein levels were reduced in both embryo fibroblasts and adult knock-out mice. The proliferation of fibroblasts derived from Day 12.5 knock out embryos was also decreased as compared to that of wild type cells.
This gene encodes an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. This protein is also a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. This protein has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been identified.
ErbB-3 binding protein 1
, ErbB3-binding protein Ebp1
, cell cycle protein p38-2G4 homolog
, erbB3-binding protein 1
, proliferation-associated protein 2G4
, ErbB3-binding protein 1
, proliferation-associated 2G4, 38kDa
, proliferation-associated protein 2G4-like
, similar to proliferation-associated 2G4, 38kD
, IRES-specific cellular trans-acting factor 45 kDa
, proliferation-associated 2G4, 38kD
, proliferation-associated protein 1
, protein p38-2G4