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  2. 蛋白
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  4. Recombinant Saccharomyces cerevisiae [PIN+] prion protein RNQ1 (RNQ1)

Recombinant Saccharomyces cerevisiae [PIN+] prion protein RNQ1 (RNQ1)

  • 中文名稱：
    釀酒酵母RNQ1重組蛋白
  • 貨號(hào)：
    CSB-YP340693SVG
  • 規(guī)格：
  • 來源：
    Yeast
  • 其他：
  • 中文名稱：
    釀酒酵母RNQ1重組蛋白
  • 貨號(hào)：
    CSB-EP340693SVG
  • 規(guī)格：
  • 來源：
    E.coli
  • 其他：
  • 中文名稱：
    釀酒酵母RNQ1重組蛋白
  • 貨號(hào)：
    CSB-EP340693SVG-B
  • 規(guī)格：
  • 來源：
    E.coli
  • 共軛：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 中文名稱：
    釀酒酵母RNQ1重組蛋白
  • 貨號(hào)：
    CSB-BP340693SVG
  • 規(guī)格：
  • 來源：
    Baculovirus
  • 其他：
  • 中文名稱：
    釀酒酵母RNQ1重組蛋白
  • 貨號(hào)：
    CSB-MP340693SVG
  • 規(guī)格：
  • 來源：
    Mammalian cell
  • 其他：

產(chǎn)品詳情

  • 純度：
    >85% (SDS-PAGE)
  • 基因名：
    RNQ1
  • Uniprot No.：
  • 別名：
    RNQ1; YCL028W; YCL181; YCL28W; [PIN+] prion protein RNQ1; Rich in asparagine and glutamine protein 1
  • 種屬：
    Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
  • 蛋白長(zhǎng)度：
    full length protein
  • 表達(dá)區(qū)域：
    1-405
  • 氨基酸序列
    MDTDKLISEA ESHFSQGNHA EAVAKLTSAA QSNPNDEQMS TIESLIQKIA GYVMDNRSGG SDASQDRAAG GGSSFMNTLM ADSKGSSQTQ LGKLALLATV MTHSSNKGSS NRGFDVGTVM SMLSGSGGGS QSMGASGLAA LASQFFKSGN NSQGQGQGQG QGQGQGQGQG QGSFTALASL ASSFMNSNNN NQQGQNQSSG GSSFGALASM ASSFMHSNNN QNSNNSQQGY NQSYQNGNQN SQGYNNQQYQ GGNGGYQQQQ GQSGGAFSSL ASMAQSYLGG GQTQSNQQQY NQQGQNNQQQ YQQQGQNYQH QQQGQQQQQG HSSSFSALAS MASSYLGNNS NSNSSYGGQQ QANEYGRPQQ NGQQQSNEYG RPQYGGNQNS NGQHESFNFS GNFSQQNNNG NQNRY
  • 蛋白標(biāo)簽：
    Tag?type?will?be?determined?during?the?manufacturing?process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 產(chǎn)品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 復(fù)溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 儲(chǔ)存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 貨期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事項(xiàng)：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

  • 功能：
    Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
  • 基因功能參考文獻(xiàn)：
    1. concluded that slow decoding of particular codons induces defects in protein homeostasis that interfere with key steps in cytokinesis and nuclear segregation PMID: 28281930
    2. results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI;(+)] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). PMID: 28537243
    3. Taking into account the earlier reports of the beneficial effect of expression of N-wt-Htt on the aggregation of mutant huntingtin, the function of wild-type huntingtin as an inhibitor of protein aggregation in the cell needs to be explored. PMID: 26628321
    4. the presence of [SWI+] can affect the interactions between Sup35 and Rnq1 during [PSI+] initiation and maturation process PMID: 24727082
    5. Study describes a spectrum of prion variants occurring naturally in wild yeast. all of the [RNQ+] variants characterized were efficient inducers of [PSI+], but differed in the subset of [PSI+] variants that formed and [RNQ+] structures can be modified after inducing, or interacting with, [PSI+] and in some cases, this interaction resulted in the loss of [RNQ+]. PMID: 24673812
    6. Polymorphism of RNQ1 was selected to protect cells from detrimental effects of the [PIN+] prion. PMID: 22949655
    7. Data indicate that the majority of mutated residues are mapped to the surface, and on one side, of contiguous alpha-helices of the nonprion domain of Rnq1, suggesting its involvement in interactions with a prion or a factor necessary for prion developmentt PMID: 21453425
    8. Data suggest that transient Hsp104 overproduction enhances prion generation through persistent effects on Rnq1 amyloid, as well as by disassembly of amorphous Ure2 aggregates, driving the aggregation toward the amyloid pathway. PMID: 21467567
    9. polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis PMID: 20224794
    10. Differences exist in the ability of the [RNQ(+)] prion variants to faithfully propagate themselves and to template the aggregation of other proteins. PMID: 20442412
    11. These findings indicate that the N-terminal non-prion domain of Rnq1 harbors a potent activity to regulate the maintenance of the [PIN(+)] prion. PMID: 20009538
    12. The [RNQ1Delta100(+)] prion demonstrates selfish activity to eliminate a heterologous prion in S. cerevisiae, showing the first instance of a selfish prion variant in living organisms. PMID: 19371377
    13. Rnq1 encompasses multiple prion determinants that can independently drive amyloid formation in vitro. PMID: 20107602
    14. Data show that increasing heat-shock protein 40 chaperone Sis1 activity before Rnq1-GFP expression, shifted Rnq1-GFP aggregation from the cytosol to the nucleus. PMID: 19656852
    15. We report that a null rnq1 mutation in the yeast RNQ1 (YCL028w) prion-like gene of so far unknown function produces the doubling of spores in the asci. PMID: 16356475
    16. RNQ1 deletion reduced expression from the divergently transcribed BIK1, allowing the identification of genetic interactors with bik1. PMID: 16972090
    17. analysis of the Rnq1 prion domain cross-seeding interactions with Sup35NM PMID: 17121829
    18. Data report that, upon depletion of Sis1, as well as upon inactivation of Hsp104, Rnq1 aggregates increased in size. PMID: 17673909
    19. use of NMR methods to examine amyloid formed in vitro from recombinant Rnq1 prion domain (residues 153-405) labeled with Tyr-1-(13)C (14 residues), Leu-1-(13)C (7 residues), or Ala-3-(13)C (13 residues) PMID: 18268327
    20. the nonprion domain of Rnq1 plays a crucial role in self-regulation of the highly reactive QN-rich prion domain of Rnq1 PMID: 18332119
    21. the J-protein Sis1, the Hsp70 Ssa, and the AAA+ ATPase Hsp104, act sequentially in the fragmentation of yeast prions [PSI(+)], [RNQ(+)], and [URE3], but the threshold of Sis1 activity required for each prion varies PMID: 18955697
    22. These data are consistent with a model of [PSI+] induction caused by physical interactions between Rnq1p and Sup35p. PMID: 19324054
    23. This study supports the occurrence of in vivo cross-seeding between Sup35 and Rnq1 and provides a new tool that can be used to dissect the mechanism of the de novo appearance of prions. PMID: 19411620
    24. Results for fibrils formed by the prion protein Rnq1 support an in-register parallel beta-sheet structure, with one Rnq1 molecule per 0.47-nm beta-sheet repeat spacing. PMID: 19706519

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  • 亞細(xì)胞定位：
    Cytoplasm. Nucleus.
  • 數(shù)據(jù)庫(kù)鏈接：

    KEGG: sce:YCL028W

    STRING: 4932.YCL028W



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