Small Ubiquitin-Like Modifier (SUMO) Antikörper

Antigen: Small Ubiquitin-Like Modifier (SUMO)

Synonyme: Dm0342, DmSUMO-1, DmSmt3, SMT3, SUMO, anon-EST:Posey240, dSmt3, l(2)04493, Dmel\CG4494, CG4494

Klonalität: Polyklonal

Wirt: Kaninchen

Reaktivität: Hefe (Saccharomyces Cerevisiae)

Applikation: ELISA, Western Blot (WB), Immunpräzipitation (IP)

Produktnummer: ABIN107153

Produktbeschreibung

Weitere Bezeichnung: SUMO (Small Ubiquitin-like Modifier)

Immunogen: This purified antibody was prepared from rabbit serum after repeated immunizations with recombinant yeast SUMO protein.

Format: Lyophilized

Beschreibung: Covalent modification of cellular proteins by the ubiquitin-like modifier SUMO (small ubiquitin-like modifier) regulates various cellular processes, such as nuclear transport, signal transduction, stress responses and cell cycle progression. But, in contrast to ubiquination, sumoylation does not tag proteins for degradation by the 26S proteasome, but rather seems to enhance stability or modulate their subcellular compartmentalization. Ubiquitin-like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin. Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg8 and Apg12. Proteins of the second class include parkin, RAD23 and DSK2, are designated ubiquitin-domain proteins (UDPs). These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other. In contrast to UBLs, UDPs are not conjugated to other proteins. Once covalently attached to cellular targets, SUMO regulates protein:protein and protein:DNA interactions, as well as localization and stability of the target protein. Sumoylation occurs in most eukaryotic systems, and SUMO is highly conserved from yeast to humans. Where invertebrates have only a single SUMO gene termed SMT3, three members of the SUMO family have been identified in vertebrates: SUMO-1 and the close homologues SUMO-2 and SUMO-3. SUMO has been called SMT3 (yeast), sentrin, PIC1, GMP1 and UBL1. SUMO has been shown to bind and regulate mammalian SP-RINGs (such as Mdm2, PIAS and PML), RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, WRN, Sp100, I kappaB-alpha, Androgen receptor (AR), GLUT1/4, Drosophila Ttk69, Dorsal, CaMK, yeast Septins, and viral CMV-IE1/2, EBV-BZLF1,

Spezifität: This product is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer stated above. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum.

Anwendungen

Applikationshinweise: Recommended Dilutions: For immunoblotting a 1:1,000 dilution is recommended. A 12 kDa band corresponding to yeast SUMO is detected. Most yeast cell lysates can be used as a positive control without induction or stimulation. For ELISA a 1:1,000 to 1:5,000 dilution is recommended. Researchers should determine optimal titers for other applications. Note: This purified polyclonal antibody reacts yeast SUMO by western blot and ELISA. Although not tested, this antibody is likely functional in immunohistochemistry and immunoprecipitation.

Konzentration: 1.0 mg/ml (by UV absorbance at 280 nm)

Buffer: Stabilizer: None. Preservative: 0.01% (w/v) Sodium Azide. Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2.

Lagerung: Store vial at 4° C prior to restoration. Restore with 0.5 ml of PBS. For extended storage aliquotcontents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear afterstanding at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior toimmediate use. Expiration date is one (1) year from date of restoration.

Forschungsgebiet: Signaltransduktion, Proteasen, DNS/RNS

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

Immunoblot of SUMO-GFP fusion proteins cleaved by insect cell protein extracts. Anti-SUMO antibody, generated by immunization with recombinant yeast SUMO, was tested by immunoblot against several constructs of SUMO-GFP fusion proteins after cleavage by proteases in insect cell protein extracts. These constructs contained various linkers between the SUMO and GFP portion of the fusion proteins. Each sample was run twice. The left lanes each contain 2 ug E.coli expressed and purified SUMO-GFP fusion proteins after incubation with lysed cells (50 ug total protein) for 1 h. The right lanes contain the same fusion proteins incubated with the lysate in the presence of 2% SDS. After probing with anti-GFP antibodies the membranes were stripped of antibody using SDS-DTT solution for 30 m at 60

Publikationen

Publikationen: Chen, Ding, LeJeune et al.: "Rpb1 sumoylation in response to UV radiation or transcriptional impairment in yeast." in: PLoS ONE, Vol. 4, Issue 4, pp. e5267, 2009 (PubMed).

Trujillo, Tyler, Ye et al.: "A genetic and molecular toolbox for analyzing histone ubiquitylation and sumoylation in yeast." in: Methods (San Diego, Calif.), 2011 (PubMed).