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anti-Human CENPA Antikörper:
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Human Polyclonal CENPA Primary Antibody für DB, ICC - ABIN2668362
Logsdon, Barrey, Bassett, DeNizio, Guo, Panchenko, Dawicki-McKenna, Heun, Black: Both tails and the centromere targeting domain of CENP-A are required for centromere establishment. in The Journal of cell biology 2015
centromere assembly factors CAL1 (zeige CALCA Antikörper) and CENP-C are required for meiotic chromosome segregation, CENP-A assembly and maintenance on sperm, as well as fertility
identify two co-evolving regions, CENP-A L1 and the CAL1 (zeige CALCA Antikörper) N terminus, as critical for lineage-specific CENP-A incorporation
A novel role has been described for the histone acetyltransferase (zeige HAT Antikörper) Hat1 (zeige HAT1 Antikörper) in the CENP-A/CID assembly pathway in Drosophila melanogaster.
CENP-A assembly by its loading factor, CAL1 (zeige CALCA Antikörper), requires RNAPII-mediated transcription of the underlying DNA
The amount of Cid that is loaded during each cell cycle appears to be determined primarily by the preexisting centromeric Cid, with little flexibility for compensation of accidental losses.
CID nucleosomes are octameric in vivo and that CID dimerization is essential for correct centromere assembly.
The F box protein (zeige FBXO30 Antikörper) partner of paired (Ppa (zeige FBXL14 Antikörper)) mediates CenH3(CID) stability in Drosophila. Ppa (zeige FBXL14 Antikörper) depletion results in increased CenH3(CID) levels. Ppa (zeige FBXL14 Antikörper) physically interacts with CenH3(CID) through the CATD (zeige CTSD Antikörper)(CID) that mediates Ppa (zeige FBXL14 Antikörper)-dependent CenH3(CID) stability.
Drosophila CENP-C is essential for centromere identity.
Cid allows for contacts betwen DNA and histones and specific targeting
Results suggest that CID mislocalization promotes formation of ectopic centromeres and multicentric chromosomes, which causes chromosome missegregation, aneuploidy, and growth defects.
findings demonstrate the involvement of consensus Cdk1 (zeige CDK1 Antikörper) phosphorylation sites on Mis18 complex assembly and thus provide a rationale for cell cycle-regulated timing of Mis18 assembly and CENP-A deposition
Upon cross-linking, the entire CENPA/CENPB (zeige CENPB Antikörper)/CENPC (zeige CENPC1 Antikörper)/CENPT (zeige CENPT Antikörper) complex is nuclease (zeige DCLRE1C Antikörper)-protected over an alpha-satellite dimer that comprises the fundamental unit of centromeric chromatin. We conclude that CENPA/CENPC and CENPT (zeige CENPT Antikörper) pathways for kinetochore assembly are physically integrated over young alpha-satellite dimers.
we review our current understanding of CENP-A evolution in relation to centromere drive and discuss classical and recent advances, including new evidence implicating CENP-A chaperones in this conflict.
there is a reciprocal interdependency of CENP-A chromatin and the underlying repetitive centromere DNA sequences bound by CENP-B (zeige CENPB Antikörper) in the maintenance of human chromosome segregation.
Identify the licensing factor M18BP1 (zeige MIS18BP1 Antikörper) and the CENP-A chaperone HJURP (zeige HJURP Antikörper) as the two key targets of Cdk (zeige CDK4 Antikörper)-based inhibition sufficient for maintenance of strict cell-cycle control of CENP-A assembly.
CENP-A specifically binds alpha satellite non-coding RNAs. Loss of CENP-A does not affect transcript abundance or stability.
Evolutionarily conserved flexible ends of the CENP-A nucleosomes are essential to ensure the fidelity of the mitotic pathway.
These data implicate the insulin (zeige INS Antikörper)-FoxM1 (zeige FOXM1 Antikörper)/PLK1 (zeige PLK1 Antikörper)/CENP-A pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes.
Findings indicate that expression of the scleroderma autoantigens IFI-16 (zeige IFI16 Antikörper) and CENPs (zeige APITD1 Antikörper), which are associated with severe vascular disease, is increased in vascular progenitors and mature endothelial cells. High level, lineage-enriched expression of autoantigens may explain the striking association between clinical phenotypes and the immune targeting of specific autoantigens.
KAT7 (zeige MYST2 Antikörper)-containing acetyltransferases associating with the Mis18 complex provides competence for histone turnover/exchange activity on alphoid DNA and prevents Suv39h1 (zeige SUV39H1 Antikörper)-mediated heterochromatin invasion into centromeres.
evolutionarily conserved flexible ends of the CENP-A nucleosomes are essential to ensure the fidelity of the mitotic pathway.
CPCs maintain relatively high levels of CENP-A early in life, which is necessary for sustaining proliferation, inhibiting senescence, and promoting survival following differentiation of CPCs.
Results report that the level of CENP-A, a protein required for cell division, declines precipitously with age in an islet-specific manner.
Cenpa, Cenpb (zeige CENPB Antikörper), and Bub3 (zeige BUB3 Antikörper), but not Cenpc (zeige CENPC1 Antikörper), interacted with PARP-1 (zeige PARP1 Antikörper)
The centromere-targeting domain of CENP-A is both necessary and sufficient for recruitment to double-strand breaks. CENP-A accumulation at DNA breaks is enhanced by active non-homologous end-joining but does not require DNA-PKcs (zeige PRKDC Antikörper) or Ligase IV.
CENP-C (zeige CENPC1 Antikörper) and M18BP1 (zeige MIS18BP1 Antikörper) recruit HJURP (zeige HJURP Antikörper) to centromeres for new CENP-A assembly.
CENP-A assembly into chromatin requires unidentified deoxycytidine deaminase (zeige APOBEC3G Antikörper) and UNG2 (zeige CCNO Antikörper), a uracil DNA glycosylase (zeige UNG Antikörper).
CENP-A deposition at the centromeres is dependent on HJURP (zeige HJURP Antikörper).
Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. CENPA encodes a centromere protein which contains a histone H3 related histone fold domain that is required for targeting to the centromere. CENPA is proposed to be a component of a modified nucleosome or nucleosome-like structure in which it replaces 1 or both copies of conventional histone H3 in the (H3-H4)2 tetrameric core of the nucleosome particle. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
centromere autoantigen A
, centromere protein A, 17kDa
, centromere-specific histone
, histone H3-like centromeric protein A
, centrosomin A
, centromere protein, Xenopus
, centromeric histone-3 like protein
, centromere protein A