Reaktivität: Human
WB, ELISA, IHC
Wirt: Kaninchen
Polyclonal
Biotin
Applikationshinweise
This purified polyclonal antibody reacts yeast SUMO by western blot and ELISA. Although not tested, this antibody is likely functional in immunohistochemistry and immunoprecipitation. 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. 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. 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.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
Restore with deionized water (or equivalent)
Buffer
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Greenlee, Alonso, Rahman, Meednu, Davis, Tabb, Cook, Miller: "The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO." in: Cytoskeleton (Hoboken, N.J.), Vol. 75, Issue 7, pp. 290-306, (2018) (PubMed).
Kramarz, Mucha, Litwin, Barg-Wojas, Wysocki, Dziadkowiec: "DNA Damage Tolerance Pathway Choice Through Uls1 Modulation of Srs2 SUMOylation in Saccharomyces cerevisiae." in: Genetics, Vol. 206, Issue 1, pp. 513-525, (2017) (PubMed).
Meyer, Shah, Zhang, Rohrs, Rao: "Evidence for intermolecular interactions between the intracellular domains of the arabidopsis receptor-like kinase ACR4, its homologs and the Wox5 transcription factor." in: PLoS ONE, Vol. 10, Issue 3, pp. e0118861, (2016) (PubMed).
Sung, Lim, Yi, Chang, Yang, Lee, Huh: "Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast." in: Genome research, Vol. 23, Issue 4, pp. 736-46, (2013) (PubMed).
Trujillo, Tyler, Ye, Berger, Osley: "A genetic and molecular toolbox for analyzing histone ubiquitylation and sumoylation in yeast." in: Methods (San Diego, Calif.), Vol. 54, Issue 3, pp. 296-303, (2011) (PubMed).
Vizeacoumar, van Dyk, S Vizeacoumar, Cheung, Li, Sydorskyy, Case, Li, Datti, Nislow, Raught, Zhang, Frey, Bloom, Boone, Andrews: "Integrating high-throughput genetic interaction mapping and high-content screening to explore yeast spindle morphogenesis." in: The Journal of cell biology, Vol. 188, Issue 1, pp. 69-81, (2010) (PubMed).
Chen, Ding, LeJeune, Ruggiero, Li: "Rpb1 sumoylation in response to UV radiation or transcriptional impairment in yeast." in: PLoS ONE, Vol. 4, Issue 4, pp. e5267, (2009) (PubMed).
Anti SUMO Antibody recognizes SUMO. 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, IkB-a, Androgen receptor (AR), GLUT1/4, Drosophila Ttk69, Dorsal, CaMK, yeast Septins, and viral CMV-IE1/2, EBV-BZLF1, HPV/BPV-E1. These bindings implicate SUMO in the stabilization of the target proteins and/or their localization to subcellular complexes. SUMO has an apparent molecular weight of ~12kDa and human SUMO-1 (a 101 amino acid polypeptide) shares 50% sequence identity with SUMO-2 and SUMO-3 and with yeast SMT3. SUMO and ubiquitin only show about 18% homology, but both possess a common three-dimensional structure characterized by a tightly packed globular fold with b-sheets wrapped around an a-helix. Synonyms: Ubiquitin-like protein SMT3 antibody, SMT3 antibody