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Histone H2A Variant (HIS2AV) (Internal Region), (pSer137) anticorps

HIS2AV Reactivité: Drosophila melanogaster ELISA, WB Hôte: Lapin Polyclonal unconjugated
N° du produit ABIN129671
  • Antigène Tous les produits Histone H2A Variant (HIS2AV)
    Histone H2A Variant (HIS2AV)
    Épitope
    Internal Region, pSer137
    Reactivité
    Drosophila melanogaster
    Hôte
    Lapin
    Clonalité
    Polyclonal
    Application
    ELISA, Western Blotting (WB)
    Specificité
    This affinity purified anti-Histone H2AvD pS137 Antibody is directed against the phosphorylated form of Drosophila H2AvD protein at the pS137 residue. The product was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross-adsorbed against the non-phosphorylated form of the immunizing peptide. Reactivity occurs against Drosophila H2AvD pS137 protein and the antibody is specific for the phosphorylated form of the protein. Reactivity with non-phosphorylated Drosophila H2AvD is minimal by ELISA. A BLAST analysis was used to suggest little to no cross reactivity with H2AvD proteins from other sources based on a comparison using the immunizing sequence. Reactivity against homologues from other sources is not known.
    Attributs du produit
    Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. H2AvD is vital for viability, but the exact function of variant histones H2A is not known. H2A is a core component of the nucleosome, an octamer containing two molecules each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 bp of DNA. HsAvD is expressed both maternally and zygotically and is found in embryos through to adults (female only). The human homologue, H2AX, is phosphorylated by ATM protein kinase when double strand DNA breaks occur. In mouse, H2AX ''knock out'' mice have an increased incidence of cancer.
    Stérilité
    Sterile filtered
    Immunogène
    Histone H2AvD pS137 Antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids 132-141 of Drosophila melanogaster (fruit fly) H2AvD protein.
    Immunogen Type: Peptide
    Isotype
    IgG
  • Indications d'application
    Histone H2 AvD pS137 Antibody has been tested for use in ELISA and by western blot. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 14 kDa in size corresponding to phosphorylated H2 vD protein by western blotting in the appropriate Drosophila tissue or cell lysate or extract. Less than 0.2 % reactivity is observed against the non-phosphorylated form of the immunizing peptide. This antibody is phospho specific for pS137 of H2 vD protein.
    Commentaires

    Gene Name: HIS2AV

    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1.0 mg/ml
    Buffer
    0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
    Agent conservateur
    Sodium azide
    Précaution d'utilisation
    WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
    Conseil sur la manipulation
    Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature.
    Stock
    4 °C/-20 °C
    Stockage commentaire
    Store vial at 4 ° C prior to restoration. For extended storage aliquot contents and freeze at -24 ° C or below. This product is stable for several weeks at 4 ° C as an undiluted liquid. Dilute only prior to immediate use. Expiration date is one (1) year from date of opening.
    Date de péremption
    12 months
  • Lin, Wang, Lin, Rastegari, Su, Chang, Liao, Chang, Pi, Yu, Chen, Lin, Lu, Su, Tzou, Chan, Hsu: "Piwi reduction in the aged niche eliminates germline stem cells via Toll-GSK3 signaling." dans: Nature communications, Vol. 11, Issue 1, pp. 3147, (2020) (PubMed).

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    Grendler, Lowgren, Mills, Losick: "Wound-induced polyploidization is driven by Myc and supports tissue repair in the presence of DNA damage." dans: Development (Cambridge, England), Vol. 146, Issue 15, (2020) (PubMed).

    Tsakiri, Gumeni, Vougas, Pendin, Papassideri, Daga, Gorgoulis, Juhász, Scorrano, Trougakos: "Proteasome dysfunction induces excessive proteome instability and loss of mitostasis that can be mitigated by enhancing mitochondrial fusion or autophagy." dans: Autophagy, Vol. 15, Issue 10, pp. 1757-1773, (2020) (PubMed).

    Mlih, Khericha, Birdwell, West, Karpac: "A virus-acquired host cytokine controls systemic aging by antagonizing apoptosis." dans: PLoS biology, Vol. 16, Issue 7, pp. e2005796, (2019) (PubMed).

    Cosolo, Jaiswal, Csordás, Grass, Uhlirova, Classen: "JNK-dependent cell cycle stalling in G2 promotes survival and senescence-like phenotypes in tissue stress." dans: eLife, Vol. 8, (2019) (PubMed).

    Merigliano, Mascolo, La Torre, Saggio, Vernì: "Protective role of vitamin B6 (PLP) against DNA damage in Drosophila models of type 2 diabetes." dans: Scientific reports, Vol. 8, Issue 1, pp. 11432, (2018) (PubMed).

    Harumoto, Lemaitre: "Male-killing toxin in a bacterial symbiont of Drosophila." dans: Nature, Vol. 557, Issue 7704, pp. 252-255, (2018) (PubMed).

    McCarthy, Deiulio, Martin, Upadhyay, Rangan: "Tip60 complex promotes expression of a differentiation factor to regulate germline differentiation in female Drosophila." dans: Molecular biology of the cell, Vol. 29, Issue 24, pp. 2933-2945, (2018) (PubMed).

    Caridi, DAgostino, Ryu, Zapotoczny, Delabaere, Li, Khodaverdian, Amaral, Lin, Rau, Chiolo: "Nuclear F-actin and myosins drive relocalization of heterochromatic breaks." dans: Nature, Vol. 559, Issue 7712, pp. 54-60, (2018) (PubMed).

    Koehler, Perkins, Ellisman, Jones: "Pink1 and Parkin regulate Drosophila intestinal stem cell proliferation during stress and aging." dans: The Journal of cell biology, Vol. 216, Issue 8, pp. 2315-2327, (2017) (PubMed).

    Merigliano, Marzio, Renda, Somma, Gatti, Vernì: "A Role for the Twins Protein Phosphatase (PP2A-B55) in the Maintenance of Drosophila Genome Integrity." dans: Genetics, Vol. 205, Issue 3, pp. 1151-1167, (2017) (PubMed).

    Ma, Han, Song, Do, Yang, Ni, Xie: "DNA damage-induced Lok/CHK2 activation compromises germline stem cell self-renewal and lineage differentiation." dans: Development (Cambridge, England), Vol. 143, Issue 23, pp. 4312-4323, (2017) (PubMed).

    Chen, Zheng, Xiao, Zheng: "Age-associated de-repression of retrotransposons in the Drosophila fat body, its potential cause and consequence." dans: Aging cell, Vol. 15, Issue 3, pp. 542-52, (2017) (PubMed).

    Swenson, Colmenares, Strom, Costes, Karpen: "The composition and organization of Drosophila heterochromatin are heterogeneous and dynamic." dans: eLife, Vol. 5, (2017) (PubMed).

    Delabaere, Ertl, Massey, Hofley, Sohail, Bienenstock, Sebastian, Chiolo, LaRocque: "Aging impairs double-strand break repair by homologous recombination in Drosophila germ cells." dans: Aging cell, Vol. 16, Issue 2, pp. 320-328, (2017) (PubMed).

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    Upadhyay, Martino Cortez, Wong-Deyrup, Tavares, Schowalter, Flora, Hill, Nasrallah, Chittur, Rangan: "Transposon Dysregulation Modulates dWnt4 Signaling to Control Germline Stem Cell Differentiation in Drosophila." dans: PLoS genetics, Vol. 12, Issue 3, pp. e1005918, (2016) (PubMed).

    Ryu, Spatola, Delabaere, Bowlin, Hopp, Kunitake, Karpen, Chiolo: "Heterochromatic breaks move to the nuclear periphery to continue recombinational repair." dans: Nature cell biology, Vol. 17, Issue 11, pp. 1401-11, (2016) (PubMed).

  • Antigène
    Histone H2A Variant (HIS2AV)
    Autre désignation
    Histone H2AvD
    Synonymes
    anticorps 5499, anticorps CG5499, anticorps Dmel\\CG5499, anticorps H2A, anticorps H2A.F/Z, anticorps H2A.X, anticorps H2A.Z, anticorps H2AV, anticorps H2AV_DROM, anticorps H2AX, anticorps H2AZ, anticorps H2Av, anticorps H2AvD, anticorps H2a.V, anticorps H2av, anticorps H2avD, anticorps HIS, anticorps HIS2AV, anticorps HIS2AVD, anticorps His, anticorps His2, anticorps His2AV, anticorps His2AvD, anticorps HisH2Av, anticorps Hist, anticorps Hist2av, anticorps gamma-H2Av, anticorps gamma-HIS2AV, anticorps gamma-His2Av, anticorps gammaH2Av, anticorps h2AvD, anticorps his, anticorps l(3)05146, anticorps l(3)810, anticorps l(3)97Dd, anticorps l(3)L1602, anticorps Histone H2A variant, anticorps His2Av
    Sujet
    Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. H2AvD is vital for viability, but the exact function of variant histones H2A is not known. H2A is a core component of the nucleosome, an octamer containing two molecules each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 bp of DNA. HsAvD is expressed both maternally and zygotically and is found in embryos through to adults (female only). The human homologue, H2AX, is phosphorylated by ATM protein kinase when double strand DNA breaks occur. In mouse, H2AX ''knock out'' mice have an increased incidence of cancer.
    Synonyms: H2AvD protein antibody
    ID gène
    43229, 17738227
    UniProt
    P08985
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