CENP-A is a variant version of histone H3 found only at centromeres. It is phosphorylated at serine 7 during mitosis.
Centromere protein A (CENP-A) is a 17 kDa centromere-specific histone variant with 62% amino acids homology to the C-terminal of histone H3. Localized in the centromere, it plays a central role in the centromere-specific chromatin formation. The depletion of histone H3 at the CENP-A binding domain suggests CENP-A to be a possible replacement for histone H3 in the packaging process of α-satellite DNA into primary chromation structure. CENP-A is essential in the formation of specialized nucleosomes at the centromere, implicating CENP-A as a centromere-specific epigenetic marker.
Acid extracted proteins from colcemid-arrested HeLa cells
Cultured supernantant in 0.05% sodium azide
Anti-phospho-CENP-A (Ser7) Antibody, clone NL41 is a high quality Rabbit Monoclonal Antibody for the detection of phospho-CENP-A (Ser7) & has been validated in Mplex, WB, ICC.
peptide containing the sequence RRpSRK in which pS is phospho-serine corresponding to amino acid 7 of human CENP-A (centromere protein A)
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.
FUNCTION: SwissProt: P49450 # Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. SIZE: 140 amino acids; 15991 Da SUBUNIT: Forms a nucleosome-like histone octamer containing two molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and two H2A-H2B heterodimers. Nucleosomes containing CENPA also contain histone H2A variants such as macroH2A H2AFY and H2A.Z/H2AFZ. The CENPA-H4 heterotetramer is more compact and structurally more rigid than corresponding H3-H4 heterotetramers. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. Interacts directly with herpes virus HSV-1 ICP0 protein. SUBCELLULAR LOCATION: Nucleus. Centromere. Kinetochore. Note=Localizes exclusively in the kinetochore domain of centromeres. DOMAIN: SwissProt: P49450 The CATD (CENPA targeting domain) region is responsible for the more compact structure of nucleosomes containinf CENPA and is necessary and sufficient to mediate the localization into centromeres. PTM: Ubiquitinated (Probable). Interaction with herpes virus HSV-1 ICP0 protein, leads to its degradation by the proteasome pathway. & Phosphorylation of Ser-7 by Aurora-A/STK6 and Aurora-B/STK12 during prophase is required for localization of Aurora-A/STK6 and Aurora-B/STK12 at inner centromere and is essential for kinetochore function. Initial phosphorylation during prophase is mediated by Aurora-A/STK6 and is maintained by Aurora-B/STK12.DISEASE:SwissProt: P49450 # Antibodies against CENPA are present in sera from patients with autoimmune diseases that developed autoantibodies against centrosomal proteins. SIMILARITY: Belongs to the histone H3 family.
Safety Information according to GHS
Product Usage Statements
routinely evaluated by immunoblot on acid extracted proteins from colcemid-arrested HeLa cells (Catalog #17-306)
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Storage and Shipping Information
Stable for 1 year at -20°C from date of receipt. For maximum recovery of product, centrifuge the vial prior to removing the cap. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
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