Recombinant Human Radical S-adenosyl methionine domain-containing protein 2 (RSAD2)
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中文名稱：人RSAD2重組蛋白
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貨號：CSB-EP848838HU-B
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說明書：
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規格：
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來源：E.coli
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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.
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其他：
產品詳情
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純度：>85% (SDS-PAGE)
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基因名：RSAD2
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Uniprot No.：
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別名：2510004L01Rik; cig 33; CIG 5; cig-33; CIG-5; CIG33; CIG5; Cytomegalovirus induced gene 5 protein ; Cytomegalovirus-induced gene 5 protein; endoplasmic reticulum-associated; interferon-inducible; Radical S adenosyl methionine domain containing 2; Radical S-adenosyl methionine domain-containing protein 2; RSAD 2; Rsad2; RSAD2_HUMAN; RSDA-2; VIG 1; vig1; Viperin; Virus inhibitory protein; virus inhibitory protein endoplasmic reticulum associated interferon inducible
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種屬：Homo sapiens (Human)
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蛋白長度：full length protein
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表達區域：1-361
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氨基酸序列MWVLTPAAFA GKLLSVFRQP LSSLWRSLVP LFCWLRATFW LLATKRRKQQ LVLRGPDETK EEEEDPPLPT TPTSVNYHFT RQCNYKCGFC FHTAKTSFVL PLEEAKRGLL LLKEAGMEKI NFSGGEPFLQ DRGEYLGKLV RFCKVELRLP SVSIVSNGSL IRERWFQNYG EYLDILAISC DSFDEEVNVL IGRGQGKKNH VENLQKLRRW CRDYRVAFKI NSVINRFNVE EDMTEQIKAL NPVRWKVFQC LLIEGENCGE DALREAERFV IGDEEFERFL ERHKEVSCLV PESNQKMKDS YLILDEYMRF LNCRKGRKDP SKSILDVGVE EAIKFSGFDE KMFLKRGGKY IWSKADLKLD W
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蛋白標簽：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.
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儲存條件：Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保質期：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.
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注意事項：Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet ：Please contact us to get it.
產品評價
相關產品
靶點詳情
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功能：Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses, including human cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus, vesicular stomatitis virus (VSV), zika virus, and human immunodeficiency virus (HIV-1). Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.
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基因功能參考文獻：
- Study reports the identification of geranyl pyrophosphate (GPP) and farnesyl pyrophosphate (FPP), two terpene intermediates in the mevalonate pathway, as substrates of human viperin. PMID: 29251770
- Viperin is antivirally active against many different viruses from different families and has been shown to inhibit several flaviviruses. Authors summarize the current knowledge about viperin and its role in antiflavivirus defense. [Review] PMID: 30059238
- Viperin N-terminal is necessary for the interaction with Junin viral nucleoprotein. PMID: 29202415
- viperin also reduced the stability of several other viral proteins in a NS3-dependent manner, suggesting a central role of NS3 in viperin's antiflavivirus activity. PMID: 29321318
- RSAD2 and AIM2 Modulate Coxsackievirus A16 and Enterovirus A71 Replication in Neuronal Cells in Different Ways That May Be Associated with Their 5' Nontranslated Regions. PMID: 29263272
- Data suggest that CIA2B and MMS19 physically interact with C-terminus of viperin/RSAD2; CIAO1 appears to function as primary viperin-interacting protein; CIA2A binds to N-terminus of viperin in CIAO1-, CIA2B-, and MMS19-independent fashion. (CIA2B = metallochaperone CIA2B/FAM96B; MMS19 = transcription factor MMS19; CIAO1 = cytosolic iron-sulfur assembly component 1; CIA2A = metallochaperone CIA2A/Fam96a) PMID: 28615450
- Data suggest that human viperin exerts "ancient radical" SAM-dependent activity in invading bacteria such as Escherichia coli; here, expression of recombinant viperin induces dramatically elongated morphology of "host"/pathogen cells. (SAM = S-adenosylmethionine) PMID: 28708394
- Exposure to hepatitis B virus up-regulates viperin expression in vivo and in vitro in placental trophoblast, and lack of this up-regulation is associated with intrauterine transmission of hepatitis B virus. PMID: 27943419
- Viperin was localized in trophoblast cells. HCMV IE1 mRNA expression was significantly inhibited by viperin RNA interference. PMID: 25814471
- data suggested that viperin impaired respiratory syncytial virus (RSV) transmission by inhibiting virus filament formation, providing a basis for its anti-virus activity in RSV-infected cells PMID: 25433308
- Viperin inhibits viral replication by interactiing with host cell proteins and viral proteins. [review] PMID: 25997337
- These data suggest that viperin requires CIAO1 for [4Fe-4S] cluster assembly, and acts through an enzymatic, Fe-S cluster- and SAM-dependent mechanism to inhibit viral RNA synthesis. PMID: 24245804
- The data indicate that viperin is the major effector underlying the ability of HCMV to regulate cellular lipid metabolism. PMID: 23935494
- Viperin is induced following dengue virus type-2 (DENV-2) infection and has anti-viral actions requiring the C-terminal end of viperin. PMID: 23638199
- inhibits replication of respiratory syncytial virus PMID: 23018837
- viperin is a critical antiviral host protein that controls chikungunya virus infection. PMID: 23160199
- The restriction of Bunyamwera virus replication mediated by interferon is an accumulated effect of at least three interferon-stimulated genes viperin, MTAP44 and PKR. PMID: 22896602
- Viperin is now known to act in different ways in the inhibition of the replication of different viruses that employ different mechanisms and organelles in their replication cycle. [Review] PMID: 22182524
- Viperin restrict influenza H1N1 virus replication in vitro. PMID: 22377585
- Viperin is an alpha-beta protein containing iron-sulfur cluster at the center pocket. PMID: 22363738
- Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein VAP-33. PMID: 21957124
- We propose that viperin interacts with NS5A and the host factor, VAP-A, to limit hepatitis C virus replication at the replication complex. PMID: 22045669
- Data idenified two cleavage sites for RNase MRP/RNase P in the coding sequence of viperin mRNA. PMID: 21053045
- study shows human cytomegalovirus (HCMV)-induced viperin disrupts cellular metabolism to enhance infectious process; viperin interaction with vMIA resulted in viperin relocalization from endoplasmic reticulum to mitochondria PMID: 21527675
- IFITM2 and IFITM3, disrupted early steps (entry and/or uncoating) of the viral infection, viperin, ISG20, and double-stranded-RNA-activated protein kinase, inhibited steps in west nile virus and dengue virus viral proteins and/or RNA biosynthesis. PMID: 20534863
- Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteristic of the radical SAM superfamily. PMID: 20176015
- the first experimental evidence confirming that viperin is indeed a radical SAM enzyme provided. PMID: 20026307
- Viperin inhibits hepatitis C virus (HCV) by localizing to lipid droplets using a domain and mechanism similar to that used by HCV itself. PMID: 19920176
- Viperin is expressed in atherosclerosis and induced in vascular cells by inflammatory stimuli and cytomegalovirus infection PMID: 15890971
- ISG (interferon-stmiulated genese) viperin has anti-Hepatitis c virus activity in vitro; we postulate that viperin, and other ISGs, acts to limit HCV replication. PMID: 16108059
- Results identify Viperin as a tightly regulated ISGF3 target gene, which is counter-regulated by PRDI-BF1. PMID: 16849320
- poly(I:C) upregulated TLR3, thereby augmenting the primary (IFN-beta) and secondary (IDO and viperin) response genes PMID: 17626075
- Overexpression of farnesyl diphosphate synthase reverses viperin-mediated inhibition of virus production and restores normal membrane fluidity. PMID: 18005724
- This work, for the first time, provides strong evidence suggesting that viperin is a putative radical S-adenosyl-l-methionine (SAM) enzyme. PMID: 18077728
- The results suggest that even though viperin gene expression is highly induced by Japanese encephalitis virus, it is negatively regulated at the protein level to counteract its antiviral effect. PMID: 18768981
- The N-terminal amphipathic alpha-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion PMID: 19074433
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亞細胞定位：Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus. Endoplasmic reticulum. Lipid droplet. Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Note=Infection with human cytomegalovirus (HCMV) causes relocation to the Golgi apparatus and to cytoplasmic vacuoles which also contain HCMV proteins glycoprotein B and pp28. Interaction with human cytomegalovirus/HHV-5 protein vMIA/UL37 results in its relocalization from the endoplasmic reticulum to the mitochondria.
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蛋白家族：Radical SAM superfamily, RSAD2 family
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