Recombinant Saccharomyces cerevisiae Protein URE2 (URE2)

中文名稱：

釀酒酵母URE2重組蛋白
貨號：

CSB-YP340527SVG
說明書：

MSDS Datasheet
規(guī)格：
來源：

Yeast
其他：

中文名稱：

釀酒酵母URE2重組蛋白
貨號：

CSB-EP340527SVG
說明書：

MSDS Datasheet
規(guī)格：
來源：

E.coli
其他：

中文名稱：

釀酒酵母URE2重組蛋白
貨號：

CSB-EP340527SVG-B
說明書：

MSDS Datasheet
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URE2重組蛋白
貨號：

CSB-BP340527SVG
說明書：

MSDS Datasheet
規(guī)格：
來源：

Baculovirus
其他：

中文名稱：

釀酒酵母URE2重組蛋白
貨號：

CSB-MP340527SVG
說明書：

MSDS Datasheet
規(guī)格：
來源：

Mammalian cell
其他：

產(chǎn)品詳情
產(chǎn)品評價(jià)
靶點(diǎn)詳情

產(chǎn)品詳情

純度：

>85% (SDS-PAGE)
基因名：

URE2
Uniprot No.：

P23202
別名：

URE2; YNL229C; N1165Transcriptional regulator URE2; Disulfide reductase; EC 1.8.4.-; Glutathione peroxidase; EC 1.11.1.9
種屬：

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
蛋白長度：

Full Length of Mature Protein
表達(dá)區(qū)域：

2-354
氨基酸序列

MNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE
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)品評價(jià)

靶點(diǎn)詳情

功能：

Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) actvites.
基因功能參考文獻(xiàn)：
1. DnaJB6-protected yeast cells from polyglutamine toxicity and cured yeast of both [URE3] prions and weak variants of [PSI(+)] prions but not strong [PSI(+)] prions PMID: 26702057
2. study found that, in addition to Sis1,[URE3-1] is specifically dependent upon Swa2; data suggest that prion-chaperone specificity arises from the Swa2 TPR domain and supports a model where Swa2 acts through Hsp70, most likely to provide additional access points for Hsp104 to promote prion template generation PMID: 26031938
3. Proteasomal degradation of Ure2p yields amyloidogenic N-terminal peptides and a C-terminal resistant fragment. In contrast to Sup35p, fibrillar Ure2p resists proteasomal degradation. PMID: 26115123
4. The enzymatically active microgel(URE2 protein, S cerevisiae) particles show robust material properties and their porous architecture allows diffusion in and out of reactants and products. PMID: 26030507
5. A completely disordered Ure2p prion domain implies that the amyloid formation of Ure2p, and likely other Q/N-rich yeast prion proteins, is primarily driven by inter-molecular interactions. PMID: 23077577
6. Hierarchical organization in the amyloid core of yeast prion protein Ure2. PMID: 21730048
7. Data suggest that the detailed organization of the cross-beta core of Ure2p may play an important role in the efficiency of prion propagation. PMID: 21419850
8. Ure2 enter vertebrate cells by endocytotic pathways and induce apoptosis. PMID: 20824085
9. analysis of the N-terminal domain of the prion Ure2p in isolation and in its natural context PMID: 20339590
10. The GST-encoding domain of URE2 confers arsenite resistance. PMID: 20740275
11. Results suggest that a wide variety of proteins could potentially affect [URE3] formation. PMID: 19752212
12. role of Ure2p in in vivo glutathione-mediated reactive oxygen species (ROS) scavenging was shown and that the ure2 mutation could cause significant disturbance in cellular oxidant balance and increased ROS level PMID: 19777209
13. Alignment of prion-like sequences in URE2 showed 17% similarity to human APP and 27% to human PRNP, and similar values for comparison with other mammals. PMID: 15208260
14. has glutathione peroxidase activity PMID: 15371425
15. aggregated Ure2p in [URE3] yeast cells is different from the amyloid filaments generated in vitro PMID: 15456789
16. The N-terminal prion domain of the Ure2 protein is unstructured in the soluble protein and does not have a specific interaction with the C-terminal nitrogen regulation domain. PMID: 15628874
17. Ure2 protects Saccharomyces cerevisiae from heavy metal ion and oxidative cellular damage. PMID: 15806612
18. Local area electron diffraction and X-ray diffraction from partially aligned specimens showed that the 4.7A reflection is meridional and therefore the underlying structure is cross-beta. PMID: 15866740
19. Amyloid filaments of recombinant Ure2p are nearly as infectious per mass of Ure2p as extracts of [URE3] strains. PMID: 16096644
20. prion induction by both Ure2p and Ure2-21p, one of the scrambled versions of Ure2p, is clearly dependent on the length of the inducing fragment PMID: 16123127
21. Results probe the state of Cys221 in the fibrillar form of Ure2pC221 and provide structural information on the structure of Ure2p within fibrils. PMID: 16405906
22. The relationship between structure, function and folding for the yeast prion Ure2 are discussed. PMID: 16427819
23. Ure2p is able to self-assemble into insoluble fibrils with a regularly twisted morphology. PMID: 17001037
24. no evidence was found that ageing of yeast increases the frequency of URE3 prion occurrence PMID: 17133618
25. Hsp40 (Ydj1) interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils PMID: 17324933
26. Data show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3] prion propagation. PMID: 17392510
27. Results describe the conformational rearrangements that lead to the assembly of Ure2p into fibrils and the propagation of the [URE3] element in yeast. PMID: 17482207
28. cross peak intensities in 2-dimensional NMR spectra of uniformly labeled Ure2p1-89 fibrils suggests that certain portions of amino acid sequence may not participate in a rigid beta-sheet, including part of Asn-rich segment between residues 44 & 76. PMID: 17953455
29. analysis of glutathione transferase activity of the yeast prion protein Ure2 PMID: 18845158
30. J-domain point mutations that disrupt functional interactions of Ydj1p with Hsp70 abolished curing, and the J domain alone cured [URE3]. PMID: 19015537
31. the potential amyloid stretch and its preceding residue can modulate the fibril assembly of Ure2p to control the initiation of prion formation PMID: 19258323
32. Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. PMID: 19321443
33. These data suggest that soluble Ure2p oligomers and native-like Ure2p fibrils, but not amyloid fibrils, interact intimately with negatively charged lipid membranes, where they allow selective cation influx. PMID: 19383475
34. the spectra of full-length fibrils of Ure2p interestingly lead to highly resolved solid-state NMR spectra PMID: 19748512
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亞細(xì)胞定位：

Cytoplasm.
蛋白家族：

GST superfamily
數(shù)據(jù)庫鏈接：

KEGG: sce:YNL229C

STRING: 4932.YNL229C