Recombinant Human Atp-Dependent Rna Helicase Ddx3X (DDX3X) Protein (His-B2M)

Name: Recombinant Human Atp-Dependent Rna Helicase Ddx3X (DDX3X) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-04056P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) DDX3X.

Collections: Fc receptors, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Atp-Dependent Rna Helicase Ddx3X (DDX3X) Protein (His-B2M) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O00571
Target Symbol	DDX3X
Synonyms	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 System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	SHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
Expression Range	2-662aa
Protein Length	Full Length of Mature Protein
Mol. Weight	87.1kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in transcription regulation. Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity. CDKN1A up-regulation may be cell-type specific. Binds CDH1/E-cadherin promoter and represses its transcription. Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis. May positively regulate TP53 transcription. Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC). Involved in the regulation of translation initiation. Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR). This function depends on helicase activity. Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning. Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety. Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process. Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle. May activate TP53 translation. Required for endoplasmic reticulum stress-induced ATF4 mRNA translation. Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E. Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E. Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta). Potentiate MAVS/DDX58-mediated induction of IFNB in early stages of infection. Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7. Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling. Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm. May also bind IFNB promoter; the function is independent of IRF3. Involved in both stress and inflammatory responses. Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells. Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity. Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells. In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation. Cleavage by caspases may inactivate DDX3X and relieve the inhibition. Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant. ATPase and casein kinase-activating functions are mutually exclusive. May be involved in mitotic chromosome segregation.; (Microbial infection) Facilitates hepatitis C virus (HCV) replication. During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex.; (Microbial infection) Facilitates HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs. This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity.; (Microbial infection) Facilitates Zika virus (ZIKV) replication.; (Microbial infection) Facilitates Dengue virus (DENV) replication.; (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication.
Subcellular Location	Cell membrane. Nucleus. Cytoplasm. Cytoplasm, Stress granule. Inflammasome. Cell projection, lamellipodium. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	DEAD box helicase family, DDX3/DED1 subfamily
Database References	HGNC: 2745 OMIM: 300160 KEGG: hsa:1654 STRING: 9606.ENSP00000382840 UniGene: Hs.728563
Associated Diseases	Mental retardation, X-linked 102 (MRX102)
Tissue Specificity	Widely expressed. In testis, expressed in spermatids. Expressed in epidermis and liver (at protein level).

Gene Functions References

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
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
DDX3 regulates MTP gene expression and lipid homeostasis through interplay with HNF4 and SHP. PMID: 28128295
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
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
this study shows that cancer-associated DDX3X mutations drive stress granule assembly and impair global translation PMID: 27180681
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
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
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
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
Our study suggests that rottlerin exhibits its anti-cancer activity partly due to upregulation of DDX3 in hepatocellular carcinoma cells. PMID: 29203243
DDX3 may play an oncogenic role to promote tumor growth and invasion in colon cancer cells PMID: 27007150
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
The article describes RNA remodeling activity of human DDX3X and Caenorhabditis elegans LAF-1 tuned by protein concentration, RNA length, and ATP. PMID: 27546789
the role of DDX3 in sarcomas PMID: 26364611
DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signaling complexes downstream from MAVS. PMID: 27980081
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
Here, the authors show that herpes simplex virus 1 gene expression, replication, and propagation depend on optimal DDX3X protein levels. PMID: 28148788
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
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
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
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
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
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
analysis of the structural and functional core of the DDX3 subfamily of DEAD-box proteins PMID: 26598523
The DDX3 may participate in antiviral innate immunity, at least in part, by translational control of interferon-induced protein kinase (PACT). PMID: 26454002
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
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
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
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
T-cell lymphoma patients with DDX3X mutations presented a poor prognosis. PMID: 26192917
Either ligand-independent or ligand-induced EGFR phosphorylation was inhibited in lung cancer cells that strongly expressed DDX3X. PMID: 25343452
Mutations in DDX3X are a common cause of unexplained intellectual disability with gender-specific effects on Wnt signaling. PMID: 26235985
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
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
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
The DDX3-Rac1-beta-catenin regulatory axis in modulating the expression of Wnt/beta-catenin target genes. PMID: 25043297
Upon infection, the HCV 3'UTR redistributes DDX3X and IKK-alpha to speckle-like cytoplasmic structures shown to be stress granules. PMID: 25740981
Cancer-associated mutants of RNA helicase DDX3X are defective in RNA-stimulated ATP hydrolysis. PMID: 25724843
Mutations in DDX3X gene is associated with recurrent convergent evolution in chronic lymphocytic leukemia. PMID: 25377784
DDX3X, a member of DEAD-box RNA helicase, is necessary for IFN production and could inhibit DENV replication PMID: 25437271
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
Overall, these results demonstrate that DDX3 represents an intrinsic host antiviral factor that restricts hepatitis B virus transcription. PMID: 25231298
These results suggest that anti-DDX3X immunotherapy is a promising treatment option in efforts to eradicate CSC in the clinical setting. PMID: 23974721
DDX3 loss by p53 inactivation via MDM2/Slug/E-cadherin pathway promotes tumor malignancy and poor patient outcome PMID: 23584477
Host DDX3 regulates Japanese encephalitis virus replication by interacting with viral un-translated regions. PMID: 24418539
DDX3 seems to interact with the HIV-1 Tat and facilitate the Tat function. PMID: 24183723
DDX3 is a new key molecule to understand the molecular mechanism underlying RNAi pathway in mammals. PMID: 23527197
Results suggest that distinct DDX DEAD-box RNA helicases DDX3 and DDX5 cooperate to modulate the HIV-1 Rev function. PMID: 23608157
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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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