Product nameAnti-ULP-1 antibody
DescriptionRabbit polyclonal to ULP-1
Tested applicationsSuitable for: WB, ELISA, ICC/IFmore details
Species reactivityReacts with: Saccharomyces cerevisiae
Recombinant full length protein corresponding to Saccharomyces cerevisiae ULP-1 aa 1-697.
Database link: Q09353
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.
Storage bufferpH: 7.20
Preservative: 0.01% Sodium azide
Constituents: 0.42% Potassium phosphate, 0.87% Sodium chloride
Concentration information loading...
Purification notesThis product is an IgG fraction antibody purified from monospecific antiserum by a multi-step process including delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against buffer.
Our Abpromise guarantee covers the use of ab34668 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/2000. Detects a band of approximately 72.4 kDa (predicted molecular weight: 80 kDa).|
|ELISA||1/4000 - 1/20000.|
|ICC/IF||Use at an assay dependent dilution.|
RelevanceULP1, ubiquitin-like protein-specific protease 1, initially processes Smt3 and also acts as a deconjugating enzyme for Smt3 [Saccharomyces cerevisiae (Baker's yeast)]. 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. 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. Three distinct steps can be distinguished in the SUMO modification pathway: 1) activation of SUMO, 2) transfer of SUMO to the conjugating enzyme, and 3) substrate modification. Since SUMO is synthesized as a precursor protein, a maturation step precedes the activation reaction. In yeast, C terminal processing of the SUMO precursor is mediated by the processing protease ULP 1 which has an additional role in the deconjugation of SUMO-modified substrates. Mature SUMO is activated by SUMO-activating enzyme, an E1-like heterodimeric protein complex composed of Uba2 and Aos1. ULP 1 function has provided evidence that SUMO modification in yeast, as has been suspected for vertebrates, plays an important role in nucleocytoplasmic trafficking.
- Probable sentrin specific protease antibody
- Ubiquitin Like Protease antibody
Anti-ULP-1 antibody (ab34668) at 1/1000 dilution + Truncated ULP 1 fusion protein (arrow-head) with 5% non-fat dry milk in TTBS
1:1,000 dilution of HRP-labeled
Donkey anti-Rabbit IgG for 1 hour at room temperature.
Predicted band size: 80 kDa
Increasing concentrations of ULP 1 were run on SDS-PAGE and transferred onto nitrocellulose. A chemiluminescence system was used for signal detection (Roche) using a 3 seconds exposure time.
ab34668 has not yet been referenced specifically in any publications.