07-574
Anti-CENP-A Antibody
Upstate®, from rabbit
Synonym(s):
Anti-CENP-A, Anti-CenH3
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Product Name
Anti-CENP-A Antibody, Upstate®, from rabbit
biological source
rabbit
conjugate
unconjugated
antibody form
affinity purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... CENPA(1058)
Analysis Note
Control
Control Histones (from Hela cells) colcemid-treated or untreated
Control Histones (from Hela cells) colcemid-treated or untreated
routinely evaluated by immunoblot in acid extracted histones from HeLa cells
Application
Anti-CENP-A Antibody is a Rabbit Polyclonal Antibody for detection of CENP-A also known as Centromere autoantigen A & has been tested in WB.
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Cell Cycle, DNA Replication & Repair
Cell Cycle, DNA Replication & Repair
Biochem/physiol Actions
Broad species cross-reactivity is predicted.
CENP-A
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
17kDa
CENP-A is a variant version of histone H3 found only at centromeres.
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.
Immunogen
peptide (RRRSRKPEAPRRRS) corresponding to amino acids 4-17 of human CENP-A
Other Notes
Replaces: 04-205
Physical form
Affinity purified immunoglobulin in 0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide.
ImmunoAffinity Purified
Preparation Note
Stable for 1 year at 2 to 8ºC from date of receipt.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
10 - Combustible liquids
wgk
WGK 1
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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CENP-A nucleosomes localize to transcription factor hotspots and subtelomeric sites in human cancer cells.
Athwal, RK; Walkiewicz, MP; Baek, S; Fu, S; Bui, M; Camps, J; Ried, T; Sung, MH; Dalal, Y
Epigenetics & Chromatin null
Essential role of microphthalmia transcription factor for DNA replication, mitosis and genomic stability in melanoma.
Strub T, Giuliano S, Ye T, Bonet C, Keime C, Kobi D, Le Gras S, Cormont M, Ballotti R et al.
Oncogene null
Leonid Andronov et al.
Bioinformatics (Oxford, England), 34(17), 3004-3012 (2018-04-11)
Single-molecule localization microscopy (SMLM) can play an important role in integrated structural biology approaches to identify, localize and determine the 3D structure of cellular structures. While many tools exist for the 3D analysis and visualization of crystal or cryo-EM structures
Qubo Zhu et al.
The Journal of cell biology, 185(5), 827-839 (2009-06-03)
Telomeric repeat binding factor 1 (TRF1) is a component of the multiprotein complex "shelterin," which organizes the telomere into a high-order structure. TRF1 knockout embryos suffer from severe growth defects without apparent telomere dysfunction, suggesting an obligatory role for TRF1
Cell-cycle-dependent structural transitions in the human CENP-A nucleosome in vivo.
Bui, M; Dimitriadis, EK; Hoischen, C; An, E; Quenet, D; Giebe, S; Nita-Lazar, A; Diekmann et al.
Cell null
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