04-789
Anti-phospho-Histone H3 (Thr11) Antibody, clone MC83, rabbit monoclonal
culture supernatant, clone MC83, Upstate®
Synonyme(s) :
H3T11P, Histone H3 (phospho T11)
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About This Item
Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Forme d'anticorps
culture supernatant
Type de produit anticorps
primary antibodies
Clone
MC83, monoclonal
Espèces réactives
human
Fabricant/nom de marque
Upstate®
Technique(s)
inhibition assay: suitable (peptide)
multiplexing: suitable
western blot: suitable
Isotype
IgG
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Modification post-traductionnelle de la cible
phosphorylation (pThr11)
Informations sur le gène
human ... H3C1(8350)
Description générale
Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm. These modifications, which include acetylation, phosphorylation, methylation, and ubiquitin-ation, occur predominantly on the N-terminal and C-terminal tails that extend beyond the nucleosome core particle. Phosphorylation at Ser10, Ser28 and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis. In mammals, phosphorylation of Thr11 modification is restricted to the centromeric region while in plant cells, phosphorylation of Thr11 was distributed along the entire length of condensed chromosomes. Mitosis-specific phosphorylation of histone H3 at Thr11 is mediated by Dlk/ZIP kinase.
Spécificité
Broad species cross-reactivity is expected based on sequence homology. An additional unidentified band at ~40 kDa appears in some lysates.
Recognizes histone H3 phosphorylated at Thr11, Mr 17kDa.
Immunogène
Peptide containing ...KS[pT]G..., in which pT corresponds to phospho-threonine at position 11 of human histone H3
Application
Anti-phospho-Histone H3 (Thr11) Antibody, clone MC83 is a rabbit monoclonal antibody for detection of phospho-Histone H3 (Thr11) also known as H3T11P, Histone H3 (phospho T11) & has been validated in WB, PIA, Mplex.
Immunoblot Analysis:
A 1:500-1:2000 dilution of this lot detected phosphorylated histone H3 in acid extracted proteins from mitotic HeLa cells treated with colcemid, but not unmodified recombinant histone H3 (Catalog # 14-494).
Western Blot Analysis:
A 1:5,000 dilution of a previous lot detected phosphorylated histone H3 in acid extracted proteins from mitotic HeLa cells treated with colcemid, but not unmodified recombinant histone H3 (Catalog # 14-494).
Multiplexing:
Beadlyte Histone-Peptide Specificity Assay: 1:1,000-1:50,000 dilutions of a previous lot were incubated with histone H3 peptides containing various modifications conjugated to Luminex microspheres. Only the peptide containing phospho-threonine 11 was
detected (Figure C).
Peptide Inhibition Analysis: 1 μM of histone H3 peptide containing phospho-threonine 11 abolished detection of histone H3 by anti-phospho-Histone H3 (Thr11), clone MC83 in immunoblot analysis of acid extracts from
colcemid treated HeLa cells (Figure D, lane 4).
A 1:500-1:2000 dilution of this lot detected phosphorylated histone H3 in acid extracted proteins from mitotic HeLa cells treated with colcemid, but not unmodified recombinant histone H3 (Catalog # 14-494).
Western Blot Analysis:
A 1:5,000 dilution of a previous lot detected phosphorylated histone H3 in acid extracted proteins from mitotic HeLa cells treated with colcemid, but not unmodified recombinant histone H3 (Catalog # 14-494).
Multiplexing:
Beadlyte Histone-Peptide Specificity Assay: 1:1,000-1:50,000 dilutions of a previous lot were incubated with histone H3 peptides containing various modifications conjugated to Luminex microspheres. Only the peptide containing phospho-threonine 11 was
detected (Figure C).
Peptide Inhibition Analysis: 1 μM of histone H3 peptide containing phospho-threonine 11 abolished detection of histone H3 by anti-phospho-Histone H3 (Thr11), clone MC83 in immunoblot analysis of acid extracts from
colcemid treated HeLa cells (Figure D, lane 4).
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Qualité
Routinely evaluated by immunoblot analysis.
Description de la cible
17kDa
Liaison
Replaces: MABE468
Forme physique
Cultured supernantant in 0.05% sodium azide
Stockage et stabilité
Stable for 1 year at -20°C from date of receipt.
For maximum recovery of product, centrifuge the vial prior to removing the cap.
For maximum recovery of product, centrifuge the vial prior to removing the cap.
Remarque sur l'analyse
Control
HeLa acid extracts
HeLa acid extracts
Informations légales
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Clause de non-responsabilité
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.
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Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Ryan Kniewel et al.
Genetics, 207(4), 1313-1333 (2017-10-08)
Saccharomyces cerevisiae Mek1 is a CHK2/Rad53-family kinase that regulates meiotic recombination and progression upon its activation in response to DNA double-strand breaks (DSBs). The full catalog of direct Mek1 phosphorylation targets remains unknown. Here, we show that phosphorylation of histone
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