ULP1 Rabbit Polyclonal Antibody
CAT#: R1564P
ULP1 rabbit polyclonal antibody, Purified
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CNY 8,869.00
货期*
4周
规格
Specifications
Product Data | |
Applications | ELISA, WB |
Recommend Dilution | 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. |
Reactivity | Yeast |
Host | Rabbit |
Clonality | Polyclonal |
Immunogen | Prepared from rabbit serum after repeated immunizations with recombinant yeast ULP-1 protein. |
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. |
Formulation | 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01% (w/v) Sodium Azide as preservative. State: Purified State: Lyophilized purified Ig fraction. |
Reconstitution Method | Restore with 0.1 ml of deionized water (or equivalent). |
Concentration | lot specific |
Purification | Multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis. |
Conjugation | Unconjugated |
Storage Condition | Store vial at 2-8°C prior to restoration. After restoration, store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. |
Database Link | |
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 | Ubiquitin-like-specific protease 1, LPB11C, YPL020C |
Note | 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 |
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