Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum. Reactivity against ULP-1 from other sources or ULP-2 has not been determined.
Purification
Multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis.
Immunogen
Prepared from rabbit serum after repeated immunizations with recombinant yeast ULP-1 protein.
This purified polyclonal antibody reacts with yeast ULP-1 by Western blot (1/500-1: 2,000)and ELISA (1/4,000-1/20,000).
Restrictions
For Research Use only
Reconstitution
Restore with 0.1 mL of deionized water (or equivalent).
Concentration
5.0 mg/mL (by UV absorbance at 280 nm)
Buffer
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01 % (w/v) Sodium Azide as preservative.
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice
Dilute only prior to immediate use. Avoid cycles of freezing and thawing.
Storage
-20 °C
Storage Comment
Store vial at -20 °C prior to opening. Centrifuge product if not completely clear after standing at room temperature. For extended storage aliquot contents and freeze at -20 °C or below.
Target
ULP1
Alternative Name
ULP1
Background
ULP-1, 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 Ulp1, 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. Ulp1 function has provided evidence that SUMO modification in yeast, as has been suspected for vertebrates, plays an important role in nucleocytoplasmic trafficking.Synonyms: LPB11C, Ubiquitin-like-specific protease 1, YPL020C