Western Blotting (WB), Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Homologie
X, Zf, B, C, Ha, Pr, Pig
Purification
This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogène
This SUMO2/3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 49-81 amino acids from the C-terminal region of human SUMO2/3.
SUMO2/3
Reactivité: Humain
WB, FACS, IF (cc), IF (p)
Hôte: Lapin
Polyclonal
Alexa Fluor 488
Indications d'application
IF: 1:100. IF: 1:100. WB: 1:2000. IHC-P: 1:50~100
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
Stockage commentaire
Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Date de péremption
6 months
Higginbotham, OShea: "Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains." dans: Journal of virology, Vol. 89, Issue 20, pp. 10260-72, (2015) (PubMed).
Myles, Fontecilla, Valdez, Vithayathil, Naik, Belkaid, Ouyang, Datta: "Signaling via the IL-20 receptor inhibits cutaneous production of IL-1β and IL-17A to promote infection with methicillin-resistant Staphylococcus aureus." dans: Nature immunology, Vol. 14, Issue 8, pp. 804-11, (2013) (PubMed).
Heo, Lee, Nigro, Thomas, Le, Chang, McClain, Reinhart-King, King, Berk, Fujiwara, Woo, Abe: "PKC? mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation." dans: The Journal of cell biology, Vol. 193, Issue 5, pp. 867-84, (2011) (PubMed).
Nadtochiy, Redman, Rahman, Brookes: "Lysine deacetylation in ischaemic preconditioning: the role of SIRT1." dans: Cardiovascular research, Vol. 89, Issue 3, pp. 643-9, (2011) (PubMed).
Snider, Weerasinghe, Iñiguez-Lluhí, Herrmann, Omary: "Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation." dans: The Journal of biological chemistry, Vol. 286, Issue 3, pp. 2273-84, (2011) (PubMed).
Cho, Yi, Tserentsoodol, Searle, Ferreira: "Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress." dans: Disease models & mechanisms, Vol. 3, Issue 9-10, pp. 595-604, (2010) (PubMed).
Martin, Schwamborn, Urlaub, Gan, Guan, Dejean: "Spatial interplay between PIASy and FIP200 in the regulation of signal transduction and transcriptional activity." dans: Molecular and cellular biology, Vol. 28, Issue 8, pp. 2771-81, (2008) (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).
Antigène
SUMO2/3
(Small Ubiquitin Related Modifier 2/3 (SUMO2/3))
anticorps SUMO2, anticorps small ubiquitin-like modifier 2, anticorps SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)-like, anticorps small ubiquitin-related modifier 2, anticorps SUMO2, anticorps LOC711990, anticorps LOC714892
Sujet
SUMO2 and SUMO3 are members of the SUMO (small ubiquitin-like modifier) protein family. This protein family functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. In vertebrates, three members of the SUMO family have been described, SUMO 1 and the functionally distinct homologues SUMO 2 and SUMO 3. SUMO modification sites present in the N terminal regions of SUMO 2 and SUMO 3 are utilized by SAE1/SAE2 (SUMO E1) and Ubc9 (SUMO E2) to form polymeric chains of SUMO 2 and SUMO 3 on protein substrates, a property not shared by SUMO 1.