Small Ubiquitin-like Modifier (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\nubiquitin 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,\nPIAS 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\ncomplexes. 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. Applications: \nSuitable for use in ELISA and Western Blot. Other applications not tested.\n\nRecommended Dilution: \nELISA: 1:1000-1:5000\nWestern Blot: 1:1000 (12kD)\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nLyophilized powder may be stored at 4 degrees C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S1014-58W1

Size

500ug

Applications

ELISA, WB

Hosts

Rabbit

Reactivities

Yeast/Fun

Form

Supplied as a lyophilized powder in PBS, pH 7.2, 0.1% sodium azide. Reconstitution: Reconstitute with 500ul sterile, PBS or sterile 40-50% glycerol for long term storage. No stabilizing proteins added.

P Type

Pab

Purity

Purified by delipidation, salt fractionation and ion exchange chromatography.

Isotype

IgG

References

Muller, S. , Hoege, C. , Pyrowolakis, G. and Jentsch, S. (2001) SUMO, ubiquitin's mysterious cousin. Nat Rev Mol Cell Biol, 2(3): 202-10.\nHochstrasser, M. (2001) SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell, 107(1): 5-8.\nKahyo, T.,Nishida, T. and Yasuda, H. (2001) Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol Cell, 8(3) 713-8.\nTakahashi, Y., Kahyo, T., Toh-E, A.,Yasuda, H. and Kikuchi, Y. (2001) Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components\nand functions as an adaptor between conjugating enzyme and substrates. J Biol Chem 276(52): 48973-7.\nYeh, E.T., Gong, L. and Kamitani, T. (2000) Ubiquitin-like proteins: new wines in new bottles. Gene, 248(1-2):1-14.\nKeane, M.M., Ettenberg, S.A., Nau, M.M., Banerjee, P., Cuello, M., Penninger, J., and Lipkowitz, S. (1999) cbl-3: a new mammalian cbl family\nprotein. Oncogene, 18(22):3365-75.

Additional Info

Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum.