CENPJ Antibody

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Description

2.1. Centrosome and Cell Cycle Studies

CENPJ antibodies are critical for investigating centrosome biogenesis and spindle assembly during mitosis. For example, studies using this antibody have shown:

  • Disruption of centrosome duplication in mice with Cenpj mutations leads to microcephaly and defective spindle formation .

  • CENPJ knockdown in cortical progenitors causes spindle misorientation, impairing neuronal migration .

2.2. Disease Modeling

The antibody has been employed to study primary autosomal recessive microcephaly (PARM), where CENPJ mutations impair brain development. Research highlights:

  • Mutations in CENPJ (e.g., splice acceptor defects) result in truncated proteins that fail to regulate centriole biogenesis .

  • Immunohistochemical staining of Cenpj in mouse embryos reveals defects in retinal neuroblast layer development .

2.3. Immunofluorescence and Colocalization

In IF assays, the antibody helps visualize centrosome dynamics. For instance:

  • CENPJ colocalizes with microtubules in dividing cells, confirming its role in spindle assembly .

  • Knockdown experiments using this antibody demonstrated delayed neuronal migration due to stabilized microtubules .

3.1. Centrosome Biogenesis

  • A study using this antibody identified CENPJ as a scaffold for centriole duplication complexes, including Cnn, Asl, and PCNT proteins .

  • Cenpj knockout in mice caused hypoalbuminemia, glucose intolerance, and increased CD8+ T cells .

3.2. Neuronal Development

  • In cortical progenitors, Cenpj knockdown disrupted spindle orientation, while rescue experiments restored normal mitosis .

  • Post-mitotic neurons lacking Cenpj exhibited aberrant centrosome positioning and reduced neuronal migration .

3.3. Cancer and Centrosome Abnormalities

  • Overexpression of CENPJ has been linked to centrosome amplification in cancer cells, a phenotype detectable via this antibody .

Protocols and Optimization

The manufacturer recommends titrating the antibody for optimal performance. Example protocols:

  • WB: Load 30–50 μg of lysate per lane; use 1:500–1:1000 dilution.

  • IF: Fix cells with 4% PFA, permeabilize with 0.1% Triton X-100, and incubate with antibody at 1:200–1:800 overnight .

Product Specs

Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze/thaw cycles.
Lead Time
Typically, we can ship products within 1-3 business days after receiving your order. Delivery time may vary depending on the purchase method or location. Please consult your local distributors for specific delivery time information.
Synonyms
BM032 antibody; CENP-J antibody; CENPJ antibody; CENPJ_HUMAN antibody; Centromere protein J antibody; Centrosomal P4.1-associated protein antibody; CPAP antibody; LAG-3-associated protein antibody; LAP antibody; LIP1 antibody; LYST interacting protein LIP1 antibody; LYST interacting protein LIP7 antibody; LYST-interacting protein 1 antibody; MCPH6 antibody; Sas 4 antibody; SASS4 antibody; SCKL4 antibody
Target Names
CENPJ
Uniprot No.

Target Background

Function
CPAP plays a critical role in cell division and centrosome function by participating in centriole duplication. It inhibits microtubule nucleation from the centrosome. CPAP is involved in regulating the slow processive growth of centriolar microtubules and acts as a microtubule plus-end tracking protein. This protein stabilizes centriolar microtubules, inhibits microtubule polymerization and extension from the distal ends of centrioles, and is essential for centriole elongation and STIL-mediated centriole amplification. CPAP is required for the recruitment of CEP295 to the proximal end of newly formed centrioles at the centriolar microtubule wall during early S phase in a PLK4-dependent manner. It may be involved in controlling centriolar-microtubule growth by acting as a regulator of tubulin release.
Gene References Into Functions
  1. CPAP regulates the delivery of its bound beta-tubulin to define the size of microtubule-based cellular structures using a "clutch-like" mechanism. PMID: 27306797
  2. Research suggests that alcohol/ethanol exposure diminishes the pool of proliferative neurons (Neuro2a cell line) by disrupting spindle orientation and promoting asymmetric cell division. These neuronal abnormalities appear to be due to reduced CENPJ protein expression levels. PMID: 29778912
  3. CPAP-S467D protein exhibits low affinity for microtubule binding but high affinity for pericentriolar material proteins. PMID: 26997271
  4. CPAP promotes timely cilium disassembly to maintain the neural progenitor pool. Mutations in CPAP cause Seckel syndrome characterized by microcephaly. PMID: 26929011
  5. Studies suggest that the single G-box domain (which appears to fold into 14-20 antiparallel beta-strands) of CENPJ has a stable but dynamic structure. CRAP forms multimers (in solution and in crystals) of elongated fibrils resembling amyloid fibrils. [REVIEW] PMID: 26517891
  6. Centrobin plays a role in the stability and centriole elongation function of CPAP, limiting centriole length. PMID: 25616662
  7. These studies provide the first structural insight into how the malfunction of centriole proteins results in human disease and also reveal that the CPAP-STIL interaction is a conserved key step in centriole biogenesis. PMID: 24052813
  8. Results showed a human-specific hypomethylation in the 5' UTR of CENPJ in the brain, where methylation levels among humans are only about one-third of those found among nonhuman primates. PMID: 24288161
  9. The Centrobin-CPAP interaction is crucial for the recruitment of CPAP to procentrioles to promote the elongation of daughter centrioles and for the persistence of CPAP on preexisting mother centrioles. PMID: 24700465
  10. CPAP depletion results in asymmetric spindle poles with uneven distribution of pericentriolar material. PMID: 24491538
  11. Sas-4 acts as a vehicle to tether PCM complexes to centrioles, independent of its known role in centriole duplication. PMID: 24385583
  12. CEP120 associates with SPICE1 and CPAP, and depletion of any of these proteins results in short procentrioles. Additionally, overexpression of CEP120 or CPAP leads to excessive centriole elongation, a process dependent on CEP120, SPICE1, and CPAP. PMID: 23810536
  13. SUMOylated CPAP can synergistically increase HBx-induced NF-kappaB activity. PMID: 23369793
  14. CEP120 is a CPAP-interacting protein that positively regulates centriole elongation. PMID: 23857771
  15. Researchers propose that CEP135 directly connects the central hub protein, hSAS-6, to the outer microtubules. This interaction is suggested to stabilize the proper cartwheel structure for subsequent CPAP-mediated centriole elongation. PMID: 23511974
  16. CPAP degradation and function are controlled by the poly(ADP-ribose) polymerase tankyrase 1. PMID: 22699936
  17. STIL and CPAP are essential for centriole formation and proper spindle position. PMID: 22100914
  18. Results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process. PMID: 21059844
  19. Data establishes that mutation of CENPJ can lead to Seckel syndrome and calls for further investigation of the role played by other microcephaly related genes in the pathogenesis of PD. PMID: 20522431
  20. Results identify centrosomal P4.1-associated protein (CPAP), a human homologue of SAS-4, as a substrate of PLK2 whose activity oscillates during the cell cycle. PMID: 20531387
  21. Cell cycle-regulated phosphorylation orchestrates the dynamics of CPAP molecular interaction and centrosome splitting to ensure genomic stability in cell division. PMID: 19889632
  22. CPAP was found to augment Stat5-mediated transcription. PMID: 12198240
  23. CPAP possesses a novel microtubule-destabilizing motif that not only inhibits microtubule nucleation from the centrosome but also depolymerizes taxol-stabilized microtubules. PMID: 15047868
  24. CPAP functions as a coactivator of NF-kappaB-mediated transcription. PMID: 15687488
  25. Mutations in the CENPJ gene are associated with autosomal recessive primary microcephaly. PMID: 15793586
  26. In summary, these findings demonstrate a structural role for CPAP in maintaining centrosome integrity and normal spindle morphology during cell division. PMID: 16316625
  27. In conclusion, these results show a direct interaction between CPAP and 14-3-3, and this interaction appears to be phosphorylation and cell cycle dependent. PMID: 16516142
  28. This study discusses CENPJ, which similarly exhibits a higher rate of protein evolution in primates compared to rodents and carnivores. PMID: 16631324
  29. High levels of LIP1 were found in the serum and synovial fluid of rheumatoid arthritis patients, providing evidence for a cytokine-like role. PMID: 18162190
  30. Mutations in this conserved sequence also eliminate d-SAS-4's microtubule-destabilizing activity, suggesting that d-SAS-4 and CPAP may play similar roles within cells. PMID: 18586240
  31. The PN2-3 fragment of CPAP is a protein with an unprecedented tubulin sequestering mechanism distinct from that of stathmin family proteins. PMID: 19131341
  32. Results suggest that CPAP and CP110 play antagonistic roles in determining the extent of tubulin addition during centriole elongation, thereby controlling the length of newly formed centrioles. PMID: 19481458
  33. Data demonstrate that CPAP is required for centrosome duplication in cycling human cells, and that CPAP overexpression results in the formation of abnormally long centrioles. PMID: 19481460
  34. Results suggest that CPAP is a novel regulator of centriole length and its intrinsic tubulin-dimer binding activity is required for procentriole elongation. PMID: 19503075
  35. This study identifies CENPJ as LYST-interacting proteins LIP1 and LIP7, which interact with the lysosomal trafficking regulator (LYST) protein. PMID: 11984006

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Database Links

HGNC: 17272

OMIM: 608393

KEGG: hsa:55835

STRING: 9606.ENSP00000371308

UniGene: Hs.513379

Involvement In Disease
Microcephaly 6, primary, autosomal recessive (MCPH6); Seckel syndrome 4 (SCKL4)
Protein Families
TCP10 family
Subcellular Location
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.

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