Rabbit anti-Human SUMO-3 Polyclonal Antibody | anti-SUMO-3 antibody

Anti-Human SUMO-3 Antibody

Cat. Num. AAA4156649

• Reactivity: Human
• Applications: Western Blot, ELISA
• Synonyms: SUMO-3; Polyclonal Antibody; Anti-Human SUMO-3 Antibody; Human SUMO-3; anti-SUMO-3 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: 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.
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)

• Applicable Applications for anti-SUMO-3 antibody: Western Blot (WB), ELISA (EIA)
• Application Notes: This purified polyclonal antibody reacts with human SUMO-3 by western blot and ELISA. Although not tested, this antibody is likely functional in immunohistochemistry and immunoprecipitation. This antibody using the specified conditions may recognize other prominent intrinsic bands (UBLs or conjugates). Other intrinsic bands are readily detectable at lower dilutions. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 11.6 kDa in size corresponding to human SUMO-3 by western blotting in the appropriate cell lysate or extract.
• Immunogen: This purified antibody was prepared from rabbit serum after repeated immunizations with recombinant human SUMO-3 protein.
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-SUMO-3 antibody

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 human. 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.