Recombinant Human Radical S-adenosyl methionine domain-containing protein 2 (RSAD2)

Code CSB-YP848838HU
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Source Yeast
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Code CSB-EP848838HU
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Source E.coli
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Code CSB-EP848838HU-B
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Source E.coli
Conjugate 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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Code CSB-BP848838HU
MSDS
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Source Baculovirus
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Code CSB-MP848838HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RSAD2
Uniprot No.
Alternative Names
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
Species
Homo sapiens (Human)
Expression Region
1-361
Target Protein Sequence
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
Protein Length
full length protein
Tag Info
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.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
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.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
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.
Notes
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.

Customer Reviews and Q&A

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Target Background

Function
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.
Gene References into Functions
  1. 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
  2. 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
  3. Viperin N-terminal is necessary for the interaction with Junin viral nucleoprotein. PMID: 29202415
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. Viperin was localized in trophoblast cells. HCMV IE1 mRNA expression was significantly inhibited by viperin RNA interference. PMID: 25814471
  10. 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
  11. Viperin inhibits viral replication by interactiing with host cell proteins and viral proteins. [review] PMID: 25997337
  12. 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
  13. The data indicate that viperin is the major effector underlying the ability of HCMV to regulate cellular lipid metabolism. PMID: 23935494
  14. 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
  15. inhibits replication of respiratory syncytial virus PMID: 23018837
  16. viperin is a critical antiviral host protein that controls chikungunya virus infection. PMID: 23160199
  17. 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
  18. 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
  19. Viperin restrict influenza H1N1 virus replication in vitro. PMID: 22377585
  20. Viperin is an alpha-beta protein containing iron-sulfur cluster at the center pocket. PMID: 22363738
  21. Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein VAP-33. PMID: 21957124
  22. 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
  23. Data idenified two cleavage sites for RNase MRP/RNase P in the coding sequence of viperin mRNA. PMID: 21053045
  24. 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
  25. 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
  26. 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
  27. the first experimental evidence confirming that viperin is indeed a radical SAM enzyme provided. PMID: 20026307
  28. 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
  29. Viperin is expressed in atherosclerosis and induced in vascular cells by inflammatory stimuli and cytomegalovirus infection PMID: 15890971
  30. 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
  31. Results identify Viperin as a tightly regulated ISGF3 target gene, which is counter-regulated by PRDI-BF1. PMID: 16849320
  32. poly(I:C) upregulated TLR3, thereby augmenting the primary (IFN-beta) and secondary (IDO and viperin) response genes PMID: 17626075
  33. Overexpression of farnesyl diphosphate synthase reverses viperin-mediated inhibition of virus production and restores normal membrane fluidity. PMID: 18005724
  34. This work, for the first time, provides strong evidence suggesting that viperin is a putative radical S-adenosyl-l-methionine (SAM) enzyme. PMID: 18077728
  35. 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
  36. 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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Subcellular Location
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.
Protein Families
Radical SAM superfamily, RSAD2 family
Database Links

HGNC: 30908

OMIM: 607810

KEGG: hsa:91543

STRING: 9606.ENSP00000371471

UniGene: Hs.17518

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