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SUMO1 anticorps (N-Term)

L’anticorps Lapin Polyclonal anti-SUMO1 a été validé pour WB, IF, FACS et IHC (p). Il convient pour détecter SUMO1 dans des échantillons de Humain. Il y a 10+ publications disponibles.
N° du produit ABIN1882136

Aperçu rapide pour SUMO1 anticorps (N-Term) (ABIN1882136)

Antigène

Voir toutes SUMO1 Anticorps
SUMO1 (Small Ubiquitin Related Modifier Protein 1 (SUMO1))

Reactivité

  • 97
  • 80
  • 74
  • 6
  • 5
  • 5
  • 4
  • 4
  • 4
  • 4
  • 3
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  • 1
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Humain

Hôte

  • 101
  • 34
  • 3
  • 1
  • 1
Lapin

Clonalité

  • 93
  • 48
Polyclonal

Conjugué

  • 73
  • 10
  • 7
  • 6
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
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  • 2
  • 2
  • 2
  • 2
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  • 1
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  • 1
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  • 1
Cet anticorp SUMO1 est non-conjugé

Application

  • 115
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Western Blotting (WB), Immunofluorescence (IF), Flow Cytometry (FACS), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))

Clone

RB0629
  • Épitope

    • 15
    • 15
    • 10
    • 8
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    • 5
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    • 1
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    • 1
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    AA 1-30, N-Term

    Homologie

    B, M, Pig, Rat

    Purification

    This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.

    Immunogène

    This SUMO1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human SUMO1.

    Isotype

    Ig Fraction
  • Indications d'application

    IF: 1:10~50. WB: 1:1000. IHC-P: 1:50~100. FC: 1:10~50

    Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.

    Agent conservateur

    Sodium azide

    Précaution d'utilisation

    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Stock

    4 °C,-20 °C

    Date de péremption

    6 months
  • Saito, Souza, Costa, Meirelles, Gonçalves, Santos, Bressan, McComb, Costello, Whelan, Kobarg: "Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects PML Nuclear Body Formation." dans: Journal of proteome research, Vol. 16, Issue 9, pp. 3147-3157, (2018) (PubMed).

    Janer, Werner, Takahashi-Fujigasaki, Daret, Fujigasaki, Takada, Duyckaerts, Brice, Dejean, Sittler: "SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7." dans: Human molecular genetics, Vol. 19, Issue 1, pp. 181-95, (2009) (PubMed).

    Ji, Degerny, Vintonenko, Deheuninck, Foveau, Leroy, Coll, Tulasne, Baert, Fafeur: "Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation." dans: Oncogene, Vol. 26, Issue 3, pp. 395-406, (2007) (PubMed).

    Bradley, van der Meer, Roodi, Yan, Chandrasekharan, Sun, Mernaugh, Parl: "Carcinogen-induced histone alteration in normal human mammary epithelial cells." dans: Carcinogenesis, Vol. 28, Issue 10, pp. 2184-92, (2007) (PubMed).

    Degerny, Monte, Beaudoin, Jaffray, Portois, Hay, de Launoit, Baert: "SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity." dans: The Journal of biological chemistry, Vol. 280, Issue 26, pp. 24330-8, (2005) (PubMed).

    Yang, Sharrocks: "SUMO promotes HDAC-mediated transcriptional repression." dans: Molecular cell, Vol. 13, Issue 4, pp. 611-7, (2004) (PubMed).

    Ling, Sankpal, Robertson, McNally, Karpova, Robertson: "Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription." dans: Nucleic acids research, Vol. 32, Issue 2, pp. 598-610, (2004) (PubMed).

    Bailey, OHare: "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1." dans: The Journal of biological chemistry, Vol. 279, Issue 1, pp. 692-703, (2003) (PubMed).

    Pountney, Huang, Burns, Haan, Thompson, Blumbergs, Gai: "SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease." dans: Experimental neurology, Vol. 184, Issue 1, pp. 436-46, (2003) (PubMed).

    Ohshima, Shimotohno: "Transforming growth factor-beta-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4." dans: The Journal of biological chemistry, Vol. 278, Issue 51, pp. 50833-42, (2003) (PubMed).

  • Antigène

    SUMO1 (Small Ubiquitin Related Modifier Protein 1 (SUMO1))

    Autre désignation

    SUMO1

    Sujet

    Covalent modification of target lysines by SUMO (small ubiquitin-like modifier) modulates processes such as protein localization, transcription, nuclear transport, mitosis, DNA replication and repair, signal transduction, and viral reproduction. SUMO does not seem to be involved in protein degradation and may in fact function as an antagonist of ubiquitin in the degradation process. The SUMO family consists of SUMO1 and closely related homologs SUMO2, SUMO3, and SUMO4. Sumoylation has been shown to regulate a wide range of proteins, including MDM2, PIAS, PML, RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, PARK2, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, CaMK, DNMT3B, TDG, HIF1A, CHD3, EXOSC9, RAD51, and viral targets such as CMV-IE1/2, EBV-BZLF1, and HPV/BPV-E1.

    Poids moléculaire

    11557

    NCBI Accession

    NP_001005781, NP_001005782, NP_003343

    UniProt

    P63165

    Pathways

    M Phase, Positive Regulation of Endopeptidase Activity, Protein targeting to Nucleus, Ubiquitin Proteasome Pathway
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