R1564P ULP1 antibody
see related secondary antibodies
0.5 mg / US$ 465
NOVUS BIOLOGICALS
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
Quick Overview
Rabbit anti ULP1
Product Description
Rabbit anti ULP1 , Presentation: Purified
Properties
| Presentation | Purified |
| Host | Rabbit |
| Catalog Number | R1564P |
| Swiss Prot. No. | Q02724 |
| Quantity | 0.5 mg |
| Price | US$ 465 |
| Delivery | Worldwide |
| Manufacturer | Acris Antibodies GmbH |
| Datasheet | view  R1564P.pdf |
Datasheet Extract
| Alternate names | Ubiquitin-like protein-specific protease 1 |
| Concentration | 5.0 mg/ml (by UV absorbance at 280 nm) |
| 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. |
| Immunogen | Prepared from rabbit serum after repeated immunizations with recombinant yeast ULP-1 protein. Swiss Num.: Q02724 |
| Format | State: Lyophilized purified Ig fraction. Purification: Multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis. BufferSystem: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01% (w/v) Sodium Azide as preservative. Reconstitution: Restore with 0.1 ml of deionized water (or equivalent). |
| Applications | 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).
Although not tested, this antibody is likely functional in Immunohistochemistry and Immunoprecipitation. Expect a band approximately 72.4 kDa in size corresponding to yeast ULP-1 by western blotting in the appropriate lysate or extract. |
| Specificity | 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. |
| Add. Information | Protein Sequence : Yeast ULP-1, 621 aa, predicted MW 72.4 kDa
1 msvevdkhrn tlqyhkknpy splfspisty rcyprvlnnp sesrrsasfs giykkrtnts 61 rfnylndrrv lsmeesmkdg sdraskagfi ggiretlwns gkylwhtfvk neprnfdgse 121 veasgnsdve srssgsrssd vpyglrenys sdtrkhkfdt stwalpnkrr riesegvgtp 181 stspisslas qksncdsdns itfsrdpfgw nkwktsaigs nsenntsdqk nsydrrqygt 241 afirkkkvak qninntklvs raqseevtyl rqifngeykv pkilkeerer qlklmdmdke 301 kdtglkksii dltekiktil iennknrlqt rnendddlvf vkekkissle rkhkdylnqk 361 lkfdrsilef ekdfkrynei lnerkkiqed lkkkkeqlak kklvpelnek dddqvqkala 421 srentqlmnr dnieitvrdf ktlaprrwln dtiieffmky iekstpntva fnsffytnls 481 ergyqgvrrw mkrkktqidk ldkiftpinl nqshwalgii dlkkktigyv dslsngpnam 541 sfailtdlqk yvmeeskhti gedfdlihld cpqqpngydc giyvcmntly gsadapldfd 601 ykdairmrrf iahliltdal k |
| Storage | Store vial at 2-8°C prior to restoration. Restore with 0.1 ml of deionized water (or equivalent). For extended storage aliquot contents and freeze at -20°C or below. Centrifuge product if not completely clear after standing at room temperature. This product is stable for one month at 2-8°C as an undiluted liquid.
Dilute only prior to immediate use. Avoid cycles of freezing and thawing. Shelf life: one year from despatch. |
| References | 1. Li S.J., Hochstrasser M. (1999) A new protease required for cell-cycle progression in yeast. Nature 398:246-251.
2. Mossessova E., Lima C.D. (2000) Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5:865-876. 3. Stade, K. et al. (2002) A Lack of SUMO Conjugation Affects cNLS-dependent Nuclear Protein Import in Yeast. J. Biol. Chem. 277(51):49554-49561. 4. Li S.J., Hochstrasser M. (2003) The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity. J.Cell Bio. 160:1069-1082. 5. Takahashi, Y., Mizoi, J., Toh-E, A. and Kikuchi, Y. (2000) Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins. J. Biochem.128 (5):723-725. |
| Pictures | Figure 1. Western blot using Affinity Purified anti-Yeast
ULP-1 antibody shows detection of a truncated ULP-1 fusion protein (arrowhead). Increasing concentrations of yeast ULP-1 were run on a SDS-PAGE, transferred onto nitrocellulose, and blocked for 1 hour with 5% non-fat dry milk in TTBS, and probed overnight at 4°C with a 1:1000 dilution of anti-yULP-1 antibody in 5% non-fat dry milk in TTBS. Detection occurred using a 1:1,000 dilution of HRP-labeled Donkey anti-Rabbit IgG for 1 hour at room temperature. A chemiluminescence system was used for signal detection (Roche) using a 3-sec exposure time. |
12 Secondary Antibodies
| Catalog No. | Name / Host | Presentation | Reactivity | ||||
|---|---|---|---|---|---|---|---|
| R1364B | Rabbit IgG (H&L) | ||||||
| Goat | Biotin | 2 mg / US$ 295 | |||||
| R1364F | Rabbit IgG (H&L) | ||||||
| Goat | FITC | 2 mg / US$ 285 | |||||
| R1364T | Rabbit IgG (H&L) | ||||||
| Goat | TRITC | 2 mg / US$ 285 | |||||
| R1364TR | Rabbit IgG (H&L) | ||||||
| Goat | Texas Red | 2 mg / US$ 295 | |||||
| R1364HRP | Rabbit IgG (H&L) | ||||||
| Goat | HRP | 2 mg / US$ 295 | |||||
| R1364AP | Rabbit IgG (H&L) | ||||||
| Goat | AP | 1 mg / US$ 325 | |||||
| R1458C2 | Rabbit IgG (H&L) multi-species ads. | ||||||
| Goat | Cy2 | 1 mg / US$ 445 | |||||
| R1458C3 | Rabbit IgG (H&L) multi-species ads. | ||||||
| Goat | Cy3 | 1 mg / US$ 445 | |||||
| R1458C35 | Rabbit IgG (H&L) multi-species ads. | ||||||
| Goat | Cy3.5 | 1 mg / US$ 445 | |||||
| R1458C5 | Rabbit IgG (H&L) multi-species ads. | ||||||
| Goat | Cy5 | 1 mg / US$ 445 | |||||
| R1458C55 | Rabbit IgG (H&L) multi-species ads. | ||||||
| Goat | Cy5.5 | 1 mg / US$ 445 | |||||
| R1427R | Rabbit IgG (H&L) F(ab')2 Fragment multi-species ads. | ||||||
| Donkey | PE | 1 ml / US$ 455 | |||||
Click here to see all secondary antibodies for 'R1564P ULP1'.
