SUMO1 antibody (N-Term)

Catalog No. ABIN1882136

The Rabbit Polyclonal anti-SUMO1 antibody has been validated for WB, IF, FACS and IHC (p). It is suitable to detect SUMO1 in samples from Human. There are 10+ publications available.

Quick Overview for SUMO1 antibody (N-Term) (ABIN1882136)

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

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This SUMO1 antibody is un-conjugated

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

Clone: RB0629

Product Details anti-SUMO1 Antibody

Binding Specificity: AA 1-30, N-Term

Predicted Reactivity: B, M, Pig, Rat

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

Immunogen: 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

Application Details

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

Restrictions: For Research Use only

Handling

Format: Liquid

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

Preservative: Sodium azide

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

Storage: 4 °C,-20 °C

Expiry Date: 6 months

References for anti-SUMO1 antibody (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." in: 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." in: 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." in: 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." in: 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." in: The Journal of biological chemistry, Vol. 280, Issue 26, pp. 24330-8, (2005) (PubMed).

Yang, Sharrocks: "SUMO promotes HDAC-mediated transcriptional repression." in: 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." in: 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." in: 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." in: 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." in: The Journal of biological chemistry, Vol. 278, Issue 51, pp. 50833-42, (2003) (PubMed).

Target Details for SUMO1

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

Alternative Name: SUMO1

Background: 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.

Molecular Weight: 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