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AB37160

Anti-DDX3 antibody

3

(1 Review)

|

(6 Publications)

Rabbit Polyclonal DDX3 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Synthetic Peptide within Human DDX3X.

View Alternative Names

DBX, DDX3, DDX3X, ATP-dependent RNA helicase DDX3X, CAP-Rf, Helicase-like protein 2, HLP2

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-DDX3 antibody (AB37160)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-DDX3 antibody (AB37160)

Immunofluorescence of DDX3 in HepG2 cells using ab37160 at 20 ug/ml.

Western blot - Anti-DDX3 antibody (AB37160)
  • WB

Unknown

Western blot - Anti-DDX3 antibody (AB37160)

Lane 1:

Western blot - Anti-DDX3 antibody (ab37160) at 0.5 µg/mL

Lane 2:

Western blot - Anti-DDX3 antibody (ab37160) at 1 µg/mL

All lanes:

Human HepG2 cell lysate at 15 µg

Predicted band size: 73 kDa

Observed band size: 73 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF

applications

Immunogen

Synthetic Peptide within Human DDX3X. The exact immunogen used to generate this antibody is proprietary information.

O00571

Specificity

Detects both DDX3 and DBY

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DDX3 also known as DEAD-box helicase 3 plays an important role mechanically as an RNA helicase involved in unwinding RNA secondary structures. The protein has a mass of approximately 73 kDa and is commonly expressed in the cytoplasm and nucleus of a wide range of cell types. Other names for DDX3 include DBX CAP-Rf and DDX3X highlighting its varied functional roles across different studies.
Biological function summary

DEAD-box helicase 3 serves as a multifunctional protein that regulates gene expression and is implicated in RNA splicing transport and translation. It forms part of various ribonucleoprotein complexes influencing processes such as mRNA export and translation initiation. DDX3 often interacts with other proteins like eIF4E which further modulates translation of specific mRNAs.

Pathways

DEAD-box helicase 3 acts as an essential component in several cellular pathways. It plays roles in the Wnt/β-catenin signaling pathway where it can influence gene transcription important for cell fate decisions. DDX3 also participates in the innate immune response pathway interacting with proteins like MAVS to modulate antiviral defense mechanisms.

DEAD-box helicase 3 has been associated with various cancers including hepatocellular carcinoma and breast cancer. Abnormal DDX3 function or expression can disrupt cell cycle regulation leading to uncontrolled cell growth. Additionally in viral infections such as Hepatitis C DDX3 interacts with viral proteins to facilitate replication showcasing its role in both promoting and hindering disease progression.

Product protocols

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Target data

Multifunctional ATP-dependent RNA helicase (PubMed : 17357160, PubMed : 21589879, PubMed : 31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed : 29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed : 17357160, PubMed : 21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed : 30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed : 16818630, PubMed : 18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed : 16818630, PubMed : 18264132). CDKN1A up-regulation may be cell-type specific (PubMed : 18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed : 18264132). 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 (PubMed : 28128295). May positively regulate TP53 transcription (PubMed : 28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed : 17095540, PubMed : 18596238). Involved in the regulation of translation initiation (PubMed : 17667941, PubMed : 18628297, PubMed : 22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed : 20837705, PubMed : 22872150). This function depends on helicase activity (PubMed : 20837705, PubMed : 22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed : 20837705). 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 (PubMed : 22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed : 22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed : 20837705). May activate TP53 translation (PubMed : 28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed : 29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed : 17667941, PubMed : 22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed : 17667941). 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) (PubMed : 20127681, PubMed : 21170385, PubMed : 31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed : 20127681, PubMed : 21170385). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed : 18583960, PubMed : 18636090, PubMed : 19913487, PubMed : 21170385, PubMed : 27980081). 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 (PubMed : 23478265). 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 (PubMed : 30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed : 30341167). 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 (PubMed : 27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed : 18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed : 21883093). 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 (By similarity). 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 (By similarity). 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 (PubMed : 18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed : 18846110). 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 (PubMed : 23413191, PubMed : 29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed : 29222110). May be involved in mitotic chromosome segregation (PubMed : 21730191).. (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed : 29899501). 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 (PubMed : 21170385).. (Microbial infection) Facilitates HIV-1 replication (PubMed : 15507209, PubMed : 18583960, PubMed : 21589879, PubMed : 22872150, PubMed : 29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed : 15507209, PubMed : 18583960, PubMed : 29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed : 18583960).. (Microbial infection) Facilitates Zika virus (ZIKV) replication.. (Microbial infection) Facilitates Dengue virus (DENV) replication.. (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication.
See full target information DDX3X

Publications (6)

Recent publications for all applications. Explore the full list and refine your search

Cancer research 79:557-571 PubMed30563889

2018

-Acting Promotes β-Catenin Signaling and Cancer Progression via DDX3-Mediated Transactivation of YY1.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Yang,Erhu Fang,Hong Mei,Yajun Chen,Huanhuan Li,Dan Li,Huajie Song,Jianqun Wang,Mei Hong,Wenjing Xiao,Xiaojing Wang,Kai Huang,Liduan Zheng,Qiangsong Tong

The Journal of clinical investigation 127:987-1004 PubMed28192372

2017

RNA-binding protein PSPC1 promotes the differentiation-dependent nuclear export of adipocyte RNAs.

Applications

Unspecified application

Species

Unspecified reactive species

Jiexin Wang,Prashant Rajbhandari,Andrey Damianov,Areum Han,Tamer Sallam,Hironori Waki,Claudio J Villanueva,Stephen D Lee,Ronni Nielsen,Susanne Mandrup,Karen Reue,Stephen G Young,Julian Whitelegge,Enrique Saez,Douglas L Black,Peter Tontonoz

Oncotarget 7:28169-82 PubMed27058758

2016

Medulloblastoma-associated DDX3 variant selectively alters the translational response to stress.

Applications

Unspecified application

Species

Unspecified reactive species

Sekyung Oh,Ryan A Flynn,Stephen N Floor,James Purzner,Lance Martin,Brian T Do,Simone Schubert,Dedeepya Vaka,Sorana Morrissy,Yisu Li,Marcel Kool,Volker Hovestadt,David T W Jones,Paul A Northcott,Thomas Risch,Hans-Jörg Warnatz,Marie-Laure Yaspo,Christopher M Adams,Ryan D Leib,Marcus Breese,Marco A Marra,David Malkin,Peter Lichter,Jennifer A Doudna,Stefan M Pfister,Michael D Taylor,Howard Y Chang,Yoon-Jae Cho

Cell death and differentiation 21:161-71 PubMed24141718

2013

Remodelling of a polypyrimidine tract-binding protein complex during apoptosis activates cellular IRESs.

Applications

Unspecified application

Species

Unspecified reactive species

H A King,L C Cobbold,X Pichon,T Pöyry,L A Wilson,H Booden,R Jukes-Jones,K Cain,K S Lilley,M Bushell,A E Willis

PloS one 7:e48702 PubMed23166591

2012

Nucleolar protein trafficking in response to HIV-1 Tat: rewiring the nucleolus.

Applications

WB

Species

Human

Mohamed Ali Jarboui,Carlo Bidoia,Elena Woods,Barbara Roe,Kieran Wynne,Giuliano Elia,William W Hall,Virginie W Gautier

Leukemia research 33:276-87 PubMed18691757

2008

Ligand-induced Flt3-downregulation modulates cell death associated proteins and enhances chemosensitivity to idarubicin in THP-1 acute myeloid leukemia cells.

Applications

WB

Species

Human

Eystein Oveland,Bjørn Tore Gjertsen,Line Wergeland,Frode Selheim,Kari E Fladmark,Randi Hovland
View all publications

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