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anti-Rat (Rattus) CENPJ Antibodies:
anti-Human CENPJ Antibodies:
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Human Polyclonal CENPJ Primary Antibody for IHC - ABIN965856
Hung, Tang, Tang: Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex. in Molecular and cellular biology 2000
Show all 3 Pubmed References
Data suggest that the single G-box domain (that appears to fold into 14-20 antiparallel beta-strands) of cenpj has stable but dynamic structure; CRAP forms multimers (in solution and in crystals) of elongated fibrils similar to amyloid fibrils. [REVIEW]
CPAP acts as a horizontal "strut" that joins the centriolar scaffold with microtubules, whereas G-box domains form perpendicular connections.
CPAP-S467D protein has a low affinity for microtubule binding but a high affinity for pericentriolar material proteins.
CPAP promotes timely cilium disassembly to maintain neural progenitor pool. CPAP mutation causes Seckel syndrome with microcephaly.
Data suggest that the single G-box domain (that appears to fold into 14-20 antiparallel beta-strands) of CENPJ has stable but dynamic structure; CRAP forms multimers (in solution and in crystals) of elongated fibrils similar to amyloid fibrils. [REVIEW]
Centrobin (show CNTROB Antibodies) plays a role in the stability and centriole elongation function of CPAP and limits the centriole length.
studies provide the first structural insight into how the malfunction of centriole proteins results in human disease and also reveal that the CPAP-STIL (show STIL Antibodies) interaction constitutes a conserved key step in centriole biogenesis
The results showed a human-specific hypomethylation in the 5' UTR (show UTS2R Antibodies) of CENPJ in the brain, where methylation levels among humans are only about one-third of those found among nonhuman primates.
Centrobin (show CNTROB Antibodies)-CPAP interaction is critical for the recruitment of CPAP to procentrioles to promote the elongation of daughter centrioles and for the persistence of CPAP on preexisting mother centrioles.
CPAP depletion results in asymmetric spindle poles with uneven distribution of pericentriolar material.
Sas-4 acts as a vehicle to tether PCM (show PCMT1 Antibodies) complexes to centrioles independent of its well-known role in centriole duplication
CEP120 (show CEP120 Antibodies) associates with SPICE1 (show SPICE1 Antibodies) and CPAP, and depletion of any of these proteins results in short procentrioles. Furthermore, CEP120 (show CEP120 Antibodies) or CPAP overexpression results in excessive centriole elongation, a process dependent on CEP120 (show CEP120 Antibodies), SPICE1 (show SPICE1 Antibodies), and CPAP.
CPAP regulates progenitor divisions and neuronal migration in the cerebral cortex downstream of Ascl1 (show ASCL1 Antibodies).
Sas4-/- mutants lack primary cilia and therefore cannot respond to Hedgehog (show SHH Antibodies) signals, but other developmental signaling pathways are normal in the mutants.
we have developed a mouse (Cenpj(tm/tm (show THBD Antibodies))) that recapitulates many of the clinical features of Seckel syndrome, thus providing clear confirmation that specific mutations of CENPJ can cause Seckel syndrome.
This gene encodes a protein that belongs to the centromere protein family. During cell division, this protein plays a structural role in the maintenance of centrosome integrity and normal spindle morphology, and it is involved in microtubule disassembly at the centrosome. This protein can function as a transcriptional coactivator in the Stat5 signaling pathway, and also as a coactivator of NF-kappaB-mediated transcription, likely via its interaction with the coactivator p300/CREB-binding protein. Mutations in this gene are associated with primary autosomal recessive microcephaly, a disorder characterized by severely reduced brain size and mental retardation. Alternatively spliced transcript variants have been found for this gene.
centromere protein J
, LAG-3-associated protein
, LYST-interacting protein 1
, LYST-interacting protein LIP1
, LYST-interacting protein LIP7
, centrosomal P4.1-associated protein