Poly(A) Binding Protein, Cytoplasmic 1 Proteine (PABPC1)

PABPC1 encodes a poly(A) binding protein. Zusätzlich bieten wir Ihnen Poly(A) Binding Protein, Cytoplasmic 1 Antikörper (78) und und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
PABPC1 26986 P11940
PABPC1 18458 P29341
PABPC1 171350 Q9EPH8
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Top Poly(A) Binding Protein, Cytoplasmic 1 Proteine auf antikoerper-online.de

Showing 7 out of 7 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 30 bis 35 Tage
$5,370.21
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Escherichia coli (E. coli) Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 30 bis 35 Tage
$5,370.21
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Escherichia coli (E. coli) Human His-SUMO Tag 100 μg Anmelden zum Anzeigen 11 Days
$411.40
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Wheat germ Human GST tag 2 μg Anmelden zum Anzeigen 11 bis 12 Tage
$338.33
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HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen Verfügbar
$814.00
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Hefe Ratte His tag   1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$3,840.83
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Escherichia coli (E. coli) Human Unkonjugiert   250 μg Anmelden zum Anzeigen 9 bis 11 Tage
$777.50
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PABPC1 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,
, , ,
Mouse (Murine)

Rat (Rattus)

Am meisten referenzierte Poly(A) Binding Protein, Cytoplasmic 1 Proteine

  1. Human PABPC1 Protein expressed in Wheat germ - ABIN1313849 : Massimelli, Majerciak, Kruhlak, Zheng: Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA. in Journal of virology 2012 (PubMed)

Weitere Proteine zu Poly(A) Binding Protein, Cytoplasmic 1 (PABPC1) Interaktionspartnern

Human Poly(A) Binding Protein, Cytoplasmic 1 (PABPC1) Interaktionspartner

  1. Study characterized the structure of multiple PABPC1 molecules bound to a long poly(A) chain as constituting a one-dimensional wormlike form. These interactions responsible for PABPC1 multimerization occur at residues in the linker region and the RNA recognition motif 2, and shown that such interaction is important for translational activity.

  2. The nicotinamide adenine dinucleotide (NAD)-dependent deacetylase SIRT1 acts as an energy sensor and negatively regulates poly(A)RNA transport via deacetylating a poly(A)-binding protein, PABP1.

  3. Epstein-Barr Virus protein EB2 first is recruited to the mRNA cap structure in the nucleus and then interacts with the proteins eIF4G and PABP to enhance the initiation step of translation.

  4. These findings identify PABPC1 as a direct regulator of cardiac hypertrophy and define a new paradigm of gene regulation in the heart, where controlled changes in poly(A) tail length influence mRNA translation.

  5. Data suggest that DEAD-box helicase 3 (DDX3X) physically interacts and co-localizes with poly(A)-binding cytoplasmic protein 1 (PABPC1) and caprin-1 in lamellipodia at the leading edge of spreading cells; these interactions are dependent on mRNA; depletion of DDX3X (via gene silencing with the CRISPR-Cas system) leads to decreased cell motility. These studies were conducted using MRC5 lung fibroblast cell line.

  6. Data suggest that hnRNPLL specifically associates with cytoplasmic PABPC1 in both T-lymphocytes and plasma cells; PABPC1 promotes binding of hnRNPLL to immunoglobulin H (IgH, heavy chain) mRNA and regulates switching from mIgH (membrane isoform) to sIgH (secreted isoform) in plasma cells. (hnRNPLL = heterogeneous nuclear ribonucleoprotein L-like protein; PABPC1 = cytoplasmic poly[A]-binding protein 1)

  7. PABP enhances the productive binding of the eRF1-eRF3 complex to the ribosome, via interactions with the N-terminal domain of eRF3a which itself has an active role in translation termination.

  8. Unr stimulated the binding of PABP1 to mRNA, and that Unr was required for the stable interaction of PABP1 and eIF4G in cells.

  9. PABPC1 decreased expression in in infertile men with non-obstructive azoospermia

  10. BTG2 stimulates mRNA deadenylation via CAF1 activation through interaction with PABPC1. Interaction of BTG2 with the first RRM domain of PABPC1 is required for BTG2 to control cell proliferation.

  11. PABPC1 is a novel co-regulator of the AR

  12. PABPC1 is upregulated in gastric carcinoma tissues, and high PABPC1 expression predicts poor survival. PABPC1 regulates proliferation and transformation of gastric cancer cells in vitro and in vivo. PABPC1 knockdown induces apoptosis.

  13. PABPC1 interacts with AGO2 and is responsible for the microRNA mediated gene silencing in high grade hepatocellular carcinoma.

  14. Poly(A) binding protein 1 enhances cap-independent translation initiation of neurovirulence factor from avian herpesvirus

  15. Metastatic duodenal cancer cells do not tolerate intracellular PABP1 accumulation and are thus exported into the extracellular milieu by the exosome-mediated pathway. In addition, PABP1 has a potential use as a biomarker for metastatic duodenal cancer.

  16. This study highlights PABP-1 as a protein that is important to the pathology of ALS and indicates that the proteomic profile of TDP-43 inclusions in ALS may differ depending on the causative genetic mutation.

  17. PABPC1 is mislocalized in spinal cord motor neurons in amyotrophic lateral sclerosis.

  18. Study shows that PABP specifically regulates iNOS mRNA stability in human DLD-1 cells by binding to different sites in the 50- and 30-UTR of the iNOS mRNA. .

  19. These results suggest that production of the NSs protein during rift valley fever virus infection leads to sequestration of PABP1 in the nuclear speckles, creating a state within the cell that favors viral protein production.

  20. These data indicate that PABPC1 is an important cellular target of human herpesvirus 8 ORF57 to directly upregulate polyadenylated nuclear RNA accumulation during viral lytic infection.

Mouse (Murine) Poly(A) Binding Protein, Cytoplasmic 1 (PABPC1) Interaktionspartner

  1. The nicotinamide adenine dinucleotide (NAD)-dependent deacetylase SIRT1 acts as an energy sensor and negatively regulates poly(A)RNA transport via deacetylating a poly(A)-binding protein, PABP1.

  2. These results suggest that PABP interacts with HuD in basal glucose conditions making translation inhibitory complex, however upon glucose stimulation this association is affected and PABP is acted upon by PDI resulting in stimulation of insulin translation.

  3. These results demonstrate that EPAB is important for oocyte-somatic communication by maintaining transzonal processes and gap junctions at the preantral stage of folliculogenesis.

  4. The authors found that the endogenous Zfp36 directly interacts with the cytoplasmic poly(A)-binding protein. Importantly, this interaction is required for the translational repression of Zfp36's target mRNAs in resolving inflammation.

  5. Data suggest that hnRNPLL specifically associates with cytoplasmic PABPC1 in both T-lymphocytes and plasma cells; PABPC1 promotes binding of hnRNPLL to immunoglobulin H (IgH, heavy chain) mRNA and regulates switching from mIgH (membrane isoform) to sIgH (secreted isoform) in plasma cells. (hnRNPLL = heterogeneous nuclear ribonucleoprotein L-like protein; PABPC1 = cytoplasmic poly[A]-binding protein 1)

  6. Superovulation with low or high doses of gonadotropins significantly altered Epab and Pabpc1 mRNA levels in GV oocytes, MII oocytes and 1- and 2-cell embryos compared with their respective controls. These changes most likely lead to variations in expression of EPAB- and PABPC1-regulated genes, which may adversely influence the quality of oocytes and early embryos retrieved using superovulation.

  7. Data (including data from studies in knockout mice) suggest that Epab (embryonic poly(A)-binding protein), which is oocyte specific, is required for ability of cumulus cells and granulosa cells to exhibit responsiveness to Egf/Egfr signaling.

  8. Epab(-/-) oocytes are smaller in size, contain peripheral germinal vesicles, and are loosely associated with cumulus cells

  9. These findings suggest that EPAB may predominantly play roles in translational regulation of the mRNAs during early oogenesis and folliculogenesis, but PABPC1 most likely perform these roles in the later terms of ovarian development along with EPAB

  10. Epab is dispensable for mouse spermatogenesis and male fertility.

  11. We analyzed the expression of sperm-specific Akap3 and the potential regulatory factors of its protein synthesis during mouse spermiogenesis.

  12. Both Epab and Pabpc1 expression increase during early postnatal life and reach their peak at D32 testis.

  13. our data support the concept that expanded ATXN2 undergoes progressive insolubility and affects PABPC1 by a toxic gain-of-function mechanism with tissue-specific effects, which may be partially alleviated by the induction of FBXW8.

  14. EPAB is necessary for oogenesis, folliculogenesis and female fertility in mice.

  15. PABPC2 was present in pachytene spermatocytes and round spermatids, whereas elongating spermatids still included PABPC1.

Poly(A) Binding Protein, Cytoplasmic 1 (PABPC1) Protein Überblick

Protein Überblick

This gene encodes a poly(A) binding protein. The protein shuttles between the nucleus and cytoplasm and binds to the 3' poly(A) tail of eukaryotic messenger RNAs via RNA-recognition motifs. The binding of this protein to poly(A) promotes ribosome recruitment and translation initiation\; it is also required for poly(A) shortening which is the first step in mRNA decay. The gene is part of a small gene family including three protein-coding genes and several pseudogenes.

Genbezeichner und Symbole assoziert mit PABPC1

  • poly(A) binding protein cytoplasmic 1 (PABPC1)
  • poly(A) binding protein, cytoplasmic 1 (Pabpc1)
  • poly(A) binding protein, cytoplasmic 1 S homeolog (pabpc1.S)
  • poly(A) binding protein, cytoplasmic 1 (pabpc1)
  • poly(A) binding protein cytoplasmic 1 like (PABPC1L)
  • poly(A) binding protein, cytoplasmic 1 L homeolog (pabpc1.L)
  • poly(A) binding protein, cytoplasmic 1a (pabpc1a)
  • poly(A) binding protein cytoplasmic 1 (Pabpc1)
  • ePAB Protein
  • pab1 Protein
  • pabp Protein
  • pabp1 Protein
  • PABPC1 Protein
  • pabpc2 Protein
  • PabpI Protein
  • Pabpl1 Protein
  • wu:fb16a02 Protein
  • wu:fi19b08 Protein
  • wu:fj12d09 Protein
  • wu:fj61f06 Protein
  • zgc:109879 Protein

Bezeichner auf Proteinebene für PABPC1

poly(A) binding protein, cytoplasmic 2 , polyadenylate-binding protein 1 , PABP-1 , poly A binding protein 1 , poly(A)-binding protein 1 , PABP 1 , PABP 1-A , PABP-1-A , PABP-A , cytoplasmic poly(A)-binding protein 1-A , poly(A)-binding protein 1-A , polyadenylate-binding protein 1-A , xPABP1-A , poly(A) binding protein, cytoplasmic 1 , polyadenylate-binding protein 1-like , PABP 1-B , PABP-1-B , PABP-B , cytoplasmic poly(A)-binding protein 1-B , poly(A)-binding protein 1-B , polyadenylate-binding protein 1-B , xPABP1-B

GENE ID SPEZIES
26986 Homo sapiens
18458 Mus musculus
171350 Rattus norvegicus
379896 Xenopus laevis
448595 Xenopus (Silurana) tropicalis
612751 Canis lupus familiaris
711882 Macaca mulatta
430997 Gallus gallus
282296 Bos taurus
432140 Xenopus laevis
606498 Danio rerio
100727743 Cavia porcellus
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