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NDP52 antibody

GTX115378
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman
TargetCALCOCO2
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Overview

  • Supplier
    GeneTex
  • Product Name
    NDP52 antibody
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:500-1:10000. ICC/IF: 1:100-1:1000. IHC-P: 1:100-1:1000. IP: 1:100-1:500. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Concentration
    1.57 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID10241
  • Target name
    CALCOCO2
  • Target description
    calcium binding and coiled-coil domain 2
  • Target synonyms
    NDP52, calcium-binding and coiled-coil domain-containing protein 2, antigen nuclear dot 52 kDa protein, nuclear domain 10 protein 52, nuclear domain 10 protein NDP52, nuclear dot protein 52
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDQ13137
  • Protein Name
    Calcium-binding and coiled-coil domain-containing protein 2
  • Scientific Description
    The protein encoded by this gene is a subunit of nuclear domain 10 (ND10) bodies. ND10 bodies are nuclear domains appearing immunohistochemically as ten dots per nucleus. They are believed to be associated with the nuclear matrix on the basis of their resistance to nuclease digestion and salt extraction. ND10 proteins are removed from the nucleus by herpes simplex virus-1 infection and may have a role in viral life cycles. [provided by RefSeq]
  • Reactivity
    Human
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Dos Santos Á, Rollins DE, Hari-Gupta Y, et al. Autophagy receptor NDP52 alters DNA conformation to modulate RNA polymerase II transcription. Nat Commun. 2023,14(1):2855. doi: 10.1038/s41467-023-38572-9
    Read this paper
  • Ke PY, Chang CW, Hsiao YC. Baicalein Activates Parkin-Dependent Mitophagy through NDP52 and OPTN. Cells. 2022,11(7). doi: 10.3390/cells11071132
    Read this paper
  • Fukushima S, Shimohata T, Inoue Y, et al. Recruitment of LC3 by Campylobacter jejuni to Bacterial Invasion Site on Host Cells via the Rac1-Mediated Signaling Pathway. Front Cell Infect Microbiol. 2022,12:829682. doi: 10.3389/fcimb.2022.829682
    Read this paper
  • Hall BS, Dos Santos SJ, Hsieh LT, et al. Inhibition of the SEC61 translocon by mycolactone induces a protective autophagic response controlled by EIF2S1-dependent translation that does not require ULK1 activity. Autophagy. 2022,18(4):841-859. doi: 10.1080/15548627.2021.1961067
    Read this paper
  • Hung CM, Lombardo PS, Malik N, et al. AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy. Sci Adv. 2021,7(15). doi: 10.1126/sciadv.abg4544
    Read this paper
  • Robichaud S, Fairman G, Vijithakumar V, et al. Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells. Autophagy. 2021,17(11):3671-3689. doi: 10.1080/15548627.2021.1886839
    Read this paper
  • Wang X, Feng L, Xin M, et al. Mechanisms underlying astrocytic connexin-43 autophagy degradation during cerebral ischemia injury and the effect on neuroinflammation and cell apoptosis. Biomed Pharmacother. 2020,127:110125. doi: 10.1016/j.biopha.2020.110125
    Read this paper
  • Ogawa M, Takada N, Shizukuishi S, et al. Streptococcus pneumoniae triggers hierarchical autophagy through reprogramming of LAPosome-like vesicles via NDP52-delocalization. Commun Biol. 2020,3(1):25. doi: 10.1038/s42003-020-0753-3
    Read this paper
  • Zachari M, Gudmundsson SR, Li Z, et al. Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform. Dev Cell. 2019,50(5):627-643.e5. doi: 10.1016/j.devcel.2019.06.016
    Read this paper
  • Liao CC, Ho MY, Liang SM, et al. Autophagic degradation of SQSTM1 inhibits ovarian cancer motility by decreasing DICER1 and AGO2 to induce MIRLET7A-3P. Autophagy. 2018,14(12):2065-2082. doi: 10.1080/15548627.2018.1501135
    Read this paper