RSAD2 Antibody
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货号:CSB-PA020536GA01HU
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规格:¥3,900
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其他:
产品详情
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Uniprot No.:Q8WXG1
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基因名:RSAD2
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别名:2510004L01Rik antibody; cig 33 antibody; CIG 5 antibody; cig-33 antibody; CIG-5 antibody; CIG33 antibody; CIG5 antibody; Cytomegalovirus induced gene 5 protein antibody; Cytomegalovirus-induced gene 5 protein antibody; endoplasmic reticulum-associated antibody; interferon-inducible antibody; Radical S adenosyl methionine domain containing 2 antibody; Radical S-adenosyl methionine domain-containing protein 2 antibody; RSAD 2 antibody; Rsad2 antibody; RSAD2_HUMAN antibody; RSDA-2 antibody; VIG 1 antibody; vig1 antibody; Viperin antibody; Virus inhibitory protein antibody; virus inhibitory protein endoplasmic reticulum associated interferon inducible antibody
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反应种属:Human,Mouse,Rat
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免疫原:Human RSAD2
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免疫原种属:Homo sapiens (Human)
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抗体亚型:IgG
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纯化方式:Antigen Affinity Purified
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浓度:It differs from different batches. Please contact us to confirm it.
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保存缓冲液:PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20oC, Avoid freeze / thaw cycles.
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产品提供形式:Liquid
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应用范围:ELISA,IF
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Protocols:
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储存条件:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
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货期:Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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靶点详情
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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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基因功能参考文献:
- 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. s 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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亚细胞定位: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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数据库链接:
HGNC: 30908
OMIM: 607810
KEGG: hsa:91543
STRING: 9606.ENSP00000371471
UniGene: Hs.17518
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