Recombinant Human ATP-dependent RNA helicase DDX3X(DDX3X)

Code CSB-YP006621HU
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Source Yeast
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Code CSB-EP006621HU-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-MP006621HU
Size Pls inquire
Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names DDX3X
Uniprot No. O00571
Alternative Names ATP dependent RNA helicase DDX3X; ATP-dependent RNA helicase DDX3X; CAP Rf; DBX; DDX14; DDX3X; DDX3X_HUMAN; DEAD (Asp Glu Ala Asp) box polypeptide 3 X linked; DEAD (Asp-Glu-Ala-Asp) box helicase 3; X-linked; DEAD box; DEAD box protein 3; DEAD box protein 3 X-chromosomal; DEAD box X isoform; DEAD box; X isoform; DEAD/H (Asp Glu Ala Asp/His) box polypeptide 3; DEAD/H box 3; DEAD/H box 3; X-linked; Helicase like protein 2; Helicase-like protein 2; HLP2; X isoform; X-chromosomal
Species Homo sapiens (Human)
Expression Region 2-662
Target Protein Sequence SHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG RSDYDGIGSR GDRSGFGKFE RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS QIYSDGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV WVEESDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW GN
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
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
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
Protein FAQs
Storage Condition Store at -20°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.

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Target Data

Function Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E
Gene References into Functions
  1. an N-terminal conserved Nuclear Export Signal (NES) is required for export of human DDX3 from the nucleus, and identified three regions within DDX3 that can independently facilitate its nuclear import. PMID: 30131165
  2. TRPV4 mediates Ca(2+) influx and nuclear accumulation of DDX3X in cells exposed to the Zika virus. Targeting of TRPV4 reduces infectivity of dengue, hepatitis C and Zika viruses. Our results highlight the role of TRPV4 in the regulation of DDX3X-dependent control of RNA metabolism and viral infectivity. PMID: 29899501
  3. DDX3 regulates MTP gene expression and lipid homeostasis through interplay with HNF4 and SHP. PMID: 28128295
  4. Through adopting the immunoprecipitation (IP), RNA immunoprecipitation (RIP), dual luciferase reporter assays, the authors illustrate that DDX3X could interact with Drosha/DGCR8 complex, elevate the processing activity of Drosha/DGCR8 complex on pri-miRNAs, and increase mature miRNA expression levels. PMID: 27586307
  5. our study suggested that DDX3 prevents generation of cancer stem cells through epigenetically regulating a subset of tumor-suppressive miRNAs expressions, which strengthens tumor suppressor role of DDX3 in hepatocellular carcinoma. PMID: 27344963
  6. this study shows that cancer-associated DDX3X mutations drive stress granule assembly and impair global translation PMID: 27180681
  7. we demonstrated that DDX3 modulated the activity of PP2A by controlling the phosphorylation of PP2A-C, which might enable PP2A-C to regulate NF-kappaB signal pathway by dephosphorylating IKK-beta. PMID: 28402257
  8. Data suggest that L protein from LCMV interactions with host proteome, specifically DDX3X, NKRF, and TRIM21. (LCMV = Lymphocytic choriomeningitis mammarenavirus; DDX3X = DEAD-box helicase 3; NKRF = NF-kappa-B-repressing factor; TRIM21 = tripartite motif-containing protein-21) PMID: 29261807
  9. DDX3 interacts extensively with RNA and ribosomal machinery to help remodel the translation landscape in response to stress, while cancer-related DDX3 variants adapt this response to selectively preserve translation PMID: 27058758
  10. Mechanistically, increased KRAS expression induced ROS production, which elevated HIF-1alpha and YAP1 expression. Increased HIF-1alpha persistently promoted DDX3 expression via a KRAS/ROS/HIF-1alpha feedback loop. PMID: 28435452
  11. Our study suggests that rottlerin exhibits its anti-cancer activity partly due to upregulation of DDX3 in hepatocellular carcinoma cells. PMID: 29203243
  12. DDX3 may play an oncogenic role to promote tumor growth and invasion in colon cancer cells PMID: 27007150
  13. Data suggest that DEAD-box helicase 3 (DDX3X) physically interacts and co-localizes with poly(A)-binding cytoplasmic protein 1 (PABPC1) and caprin-1 in lamellipodia at the leading edge of spreading cells; these interactions are dependent on mRNA; depletion of DDX3X (via gene silencing with the CRISPR-Cas system) leads to decreased cell motility. These studies were conducted using MRC5 lung fibroblast cell line. PMID: 28733330
  14. The article describes RNA remodeling activity of human DDX3X and Caenorhabditis elegans LAF-1 tuned by protein concentration, RNA length, and ATP. PMID: 27546789
  15. the role of DDX3 in sarcomas PMID: 26364611
  16. DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signaling complexes downstream from MAVS. PMID: 27980081
  17. Here we identify the DEAD-box helicase 3 (DDX3) as a novel interaction partner of Y. enterocolitica YopM and present the three-dimensional structure of a YopM:DDX3 complex PMID: 27300509
  18. Here, the authors show that herpes simplex virus 1 gene expression, replication, and propagation depend on optimal DDX3X protein levels. PMID: 28148788
  19. de novo heterozygous DDX3X variants should be considered not only in females with unexplained ID, but also in individuals with a clinical diagnosis of T-CS. PMID: 28371085
  20. high metastatic DDX3 expression correlates with worse survival, implying that DDX3 is a potential therapeutic target in metastatic breast cancer, in particular in the clinically important group of TN patients. PMID: 27999982
  21. Herein, we showed for the first time, to our knowledge, that the inhibition of DDX3 by a small molecule could be successfully exploited for the development of a broad spectrum antiviral agent. PMID: 27118832
  22. Data show that knockdown of RNA helicase DDX3 in breast cancer MCF-7 and MDA-MB-231 cells resulted in decreased proliferation rates. PMID: 26337079
  23. Our results suggest that the intrinsically disordered N-terminal domain of DDX3 regulates its functions in translation by acting prior to the recruitment of the 43S pre-initiation complex onto the viral 5'-UTR. PMID: 27012366
  24. The results do not support our hypothesis that common germline genetic variants in the DDX3X genes is associated with the risk of developing medulloblastoma. PMID: 26290144
  25. analysis of the structural and functional core of the DDX3 subfamily of DEAD-box proteins PMID: 26598523
  26. The DDX3 may participate in antiviral innate immunity, at least in part, by translational control of interferon-induced protein kinase (PACT). PMID: 26454002
  27. As such, DDX3 has been shown to play roles both upstream and downstream of I-kappa beta kinase epsilon (IKKepsilon)/TANK-binding kinase 1, leading to IFN-beta production. PMID: 26174373
  28. Data show that DEAD-box helicase 3 (DDX3) had a significant prognostic predictive power in colorectal cancer at both RNA and protein level. PMID: 26087195
  29. Taken together, our result demonstrates that Ketorolac salt is a newly discovered bioactive compound against DDX3 and this compound can be used as an ideal drug candidate to treat DDX3 associated oral cancer. PMID: 25918862
  30. Loss of DDX3 function either by shRNA or by RK-33 impaired Wnt signaling through disruption of the DDX3-beta-catenin axis and inhibited non-homologous end joining-the major DNA repair pathway in mammalian somatic cells. PMID: 25820276
  31. T-cell lymphoma patients with DDX3X mutations presented a poor prognosis. PMID: 26192917
  32. Either ligand-independent or ligand-induced EGFR phosphorylation was inhibited in lung cancer cells that strongly expressed DDX3X. PMID: 25343452
  33. Mutations in DDX3X are a common cause of unexplained intellectual disability with gender-specific effects on Wnt signaling. PMID: 26235985
  34. Data suggest complex translational control mechanism(s) for the human DDX3X gene locus functioning only in the male germ line and resulting in expression of its protein only in the postmeiotic spermatids. PMID: 25208899
  35. Low/negative DDX3 expression in tumor cells was significantly associated with aggressive clinical manifestations and might be an independent survival predictor, particularly in non-smoker patients with OSCC PMID: 23410059
  36. identification of DDX3X mutations in 10% of cases, preferentially in males (4/5 cases); analysis suggested an association between DDX3X inactivation and clinically unfavorable features and poor outcome of chronic lymphocytic leukaemia PMID: 25382417
  37. The DDX3-Rac1-beta-catenin regulatory axis in modulating the expression of Wnt/beta-catenin target genes. PMID: 25043297
  38. Upon infection, the HCV 3'UTR redistributes DDX3X and IKK-alpha to speckle-like cytoplasmic structures shown to be stress granules. PMID: 25740981
  39. Cancer-associated mutants of RNA helicase DDX3X are defective in RNA-stimulated ATP hydrolysis. PMID: 25724843
  40. Mutations in DDX3X gene is associated with recurrent convergent evolution in chronic lymphocytic leukemia. PMID: 25377784
  41. DDX3X, a member of DEAD-box RNA helicase, is necessary for IFN production and could inhibit DENV replication PMID: 25437271
  42. This review discusses the considerable body of work on the biochemistry and biology of DDX3, including the recently discovered link of human DDX3 to tumorigenesis. PMID: 25039764
  43. Overall, these results demonstrate that DDX3 represents an intrinsic host antiviral factor that restricts hepatitis B virus transcription. PMID: 25231298
  44. These results suggest that anti-DDX3X immunotherapy is a promising treatment option in efforts to eradicate CSC in the clinical setting. PMID: 23974721
  45. DDX3 loss by p53 inactivation via MDM2/Slug/E-cadherin pathway promotes tumor malignancy and poor patient outcome PMID: 23584477
  46. Host DDX3 regulates Japanese encephalitis virus replication by interacting with viral un-translated regions. PMID: 24418539
  47. DDX3 seems to interact with the HIV-1 Tat and facilitate the Tat function. PMID: 24183723
  48. DDX3 is a new key molecule to understand the molecular mechanism underlying RNAi pathway in mammals. PMID: 23527197
  49. Results suggest that distinct DDX DEAD-box RNA helicases DDX3 and DDX5 cooperate to modulate the HIV-1 Rev function. PMID: 23608157
  50. In pediatric T-acute lymphoblastic leukemia, we have identified 2 RNA processing genes, that is, HNRNPH1/5q35 and DDX3X/Xp11.3 as new MLLT10 fusion partners. PMID: 23673860

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Involvement in disease Mental retardation, X-linked 102 (MRX102)
Subcellular Location Nucleus speckle, Cytoplasm, Mitochondrion outer membrane
Protein Families DEAD box helicase family, DDX3/DED1 subfamily
Database Links

HGNC: 2745

OMIM: 300160

KEGG: hsa:1654

STRING: 9606.ENSP00000382840

UniGene: Hs.728563

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