SUMO1 anticorps (N-Term)

N° du produit ABIN1882136

Détail du produit anti-SUMO1 anticorps

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

Épitope: AA 1-30, N-Term

Reactivité: Humain

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp SUMO1 est non-conjugé

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

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.

Clone: RB0629

Isotype: Ig Fraction

Information d'application

Indications d'application: IF: 1:10~50. WB: 1:1000. IHC-P: 1:50~100. FC: 1:10~50

Restrictions: For Research Use only

Stockage

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

Références pour anticorps anti-SUMO1 (ABIN1882136)

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).

Détails sur SUMO1

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

Autre désignation: SUMO1 (SUMO1 Produits)

Synonymes: anticorps DAP1, anticorps GMP1, anticorps OFC10, anticorps PIC1, anticorps SENP2, anticorps SMT3, anticorps SMT3C, anticorps SMT3H3, anticorps UBL1, anticorps hm:zeh0670, anticorps wu:fb74c02, anticorps wu:fd12c02, anticorps zgc:65934, anticorps zgc:85634, anticorps SUMO1, anticorps dap1, anticorps gmp1, anticorps ofc10, anticorps pic1, anticorps senp2, anticorps smt3, anticorps smt3c, anticorps sumo-1, anticorps sumo1, anticorps ubl1, anticorps xsumo-1, anticorps xsumo1, anticorps ARABIDOPSIS THALIANA SMALL UBIQUITIN-LIKE MODIFIER 1, anticorps ATSUMO1, anticorps F10M23.180, anticorps F10M23_180, anticorps SMALL UBIQUITIN-LIKE MODIFIER 1, anticorps SUM1, anticorps SUMO 1, anticorps small ubiquitin-like modifier 1, anticorps pigSUMO1, anticorps SENTRIN, anticorps SMTP3, anticorps SUMO-1, anticorps Smt3C, anticorps Ubl1, anticorps small ubiquitin-like modifier 1, anticorps small ubiquitin-like modifier 1 S homeolog, anticorps small ubiquitin-related protein 1, anticorps SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae), anticorps SMT3 suppressor of mif two 3 homolog 1 (yeast), anticorps small ubiquitin-like modifier 1 L homeolog, anticorps Sumo1, anticorps SUMO1, anticorps sumo1, anticorps sumo1.S, anticorps sumo-1, anticorps sumo1.L

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