Sign in or Register   Sign in or Register
  |  

Mouse Anti-DDX17 Recombinant Antibody (1B5B09) (CBMAB-D0532-YC)

Provided herein is a Mouse monoclonal antibody, which binds to DEAD-Box Helicase 17 (DDX17). The antibody can be used for immunoassay techniques, such as WB, IF, IP.
See all DDX17 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
1B5B09
Antibody Isotype
IgG1, κ
Application
WB, IF, IP

Basic Information

Immunogen
Partial human DDX17 recombinant protein (1-107 a.a.)
Specificity
Human, Mouse
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
DEAD (Asp-Glu-Ala-Asp) box polypeptide 17
Introduction
DDX17 is a DEAD box protein, which is an ATPase activated by a variety of RNA species, but not by dsDNA. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and splicesosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division.
Entrez Gene ID
Human10521
Mouse67040
UniProt ID
HumanQ92841
MouseQ501J6
Alternative Names
DEAD-Box Helicase 17; DEAD/H (Asp-Glu-Ala-Asp/His) Box Polypeptide 17 (72kD); DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 17; DEAD (Asp-Glu-Ala-Asp) Box Helicase 17; RNA-Dependent Helicase P72; DEAD Box Protein P72; DEAD Box Protein P82;
Function
As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, ribosomal RNA processing and miRNA processing, as well as transcription regulation. Regulates the alternative splicing of exons exhibiting specific features (PubMed:12138182, PubMed:23022728, PubMed:24910439, PubMed:22266867).

For instance, promotes the inclusion of AC-rich alternative exons in CD44 transcripts (PubMed:12138182).

This function requires the RNA helicase activity (PubMed:12138182, PubMed:23022728, PubMed:24910439, PubMed:22266867).

Affects NFAT5 and histone macro-H2A.1/MACROH2A1 alternative splicing in a CDK9-dependent manner (PubMed:26209609, PubMed:22266867).

In NFAT5, promotes the introduction of alternative exon 4, which contains 2 stop codons and may target NFAT5 exon 4-containing transcripts to nonsense-mediated mRNA decay, leading to the down-regulation of NFAT5 protein (PubMed:22266867).

Affects splicing of mediators of steroid hormone signaling pathway, including kinases that phosphorylates ESR1, such as CDK2, MAPK1 and GSK3B, and transcriptional regulators, such as CREBBP, MED1, NCOR1 and NCOR2. By affecting GSK3B splicing, participates in ESR1 and AR stabilization (PubMed:24275493).

In myoblasts and epithelial cells, cooperates with HNRNPH1 to control the splicing of specific subsets of exons (PubMed:24910439).

In addition to binding mature mRNAs, also interacts with certain pri-microRNAs, including MIR663/miR-663a, MIR99B/miR-99b, and MIR6087/miR-6087 (PubMed:25126784).

Binds pri-microRNAs on the 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3' consensus sequence (PubMed:24581491).

Required for the production of subsets of microRNAs, including MIR21 and MIR125B1 (PubMed:24581491, PubMed:27478153).

May be involved not only in microRNA primary transcript processing, but also stabilization (By similarity).

Participates in MYC down-regulation at high cell density through the production of MYC-targeting microRNAs (PubMed:24581491).

Along with DDX5, may be involved in the processing of the 32S intermediate into the mature 28S ribosomal RNA (PubMed:17485482).

Promoter-specific transcription regulator, functioning as a coactivator or corepressor depending on the context of the promoter and the transcriptional complex in which it exists (PubMed:15298701).

Enhances NFAT5 transcriptional activity (PubMed:22266867).

Synergizes with TP53 in the activation of the MDM2 promoter; this activity requires acetylation on lysine residues (PubMed:17226766, PubMed:20663877, PubMed:19995069).

May also coactivate MDM2 transcription through a TP53-independent pathway (PubMed:17226766).

Coactivates MMP7 transcription (PubMed:17226766).

Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1 transcription (PubMed:17699760).

Alone or in combination with DDX5 and/or SRA1 non-coding RNA, plays a critical role in promoting the assembly of proteins required for the formation of the transcription initiation complex and chromatin remodeling leading to coactivation of MYOD1-dependent transcription. This helicase-independent activity is required for skeletal muscle cells to properly differentiate into myotubes (PubMed:17011493, PubMed:24910439).

During epithelial-to-mesenchymal transition, coregulates SMAD-dependent transcriptional activity, directly controlling key effectors of differentiation, including miRNAs which in turn directly repress its expression (PubMed:24910439).

Plays a role in estrogen and testosterone signaling pathway at several levels. Mediates the use of alternative promoters in estrogen-responsive genes and regulates transcription and splicing of a large number of steroid hormone target genes (PubMed:24275493, PubMed:20406972, PubMed:20663877, PubMed:19995069).

Contrary to splicing regulation activity, transcriptional coregulation of the estrogen receptor ESR1 is helicase-independent (PubMed:19718048, PubMed:24275493).

Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner (PubMed:25126784).

Binds to RVFV RNA, likely via structured viral RNA elements (PubMed:25126784).

Promotes mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in an ATPase-dependent manner (PubMed:18334637).
Biological Process
Alternative mRNA splicing, via spliceosome Source: UniProtKB
Androgen receptor signaling pathway Source: UniProtKB
Defense response to virus Source: UniProtKB-KW
Epithelial to mesenchymal transition Source: UniProtKB
Gene silencing by RNA Source: UniProtKB-KW
Intracellular estrogen receptor signaling pathway Source: UniProtKB
miRNA metabolic process Source: UniProtKB
Myoblast differentiation Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
Regulation of skeletal muscle cell differentiation Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: UniProtKB
RNA processing Source: ProtInc
rRNA processing Source: UniProtKB-KW
Cellular Location
Nucleus; Nucleolus; Cytosol. In the course of bunyavirus infection, relocalizes from the nucleus to the cytosol where it binds viral RNA to antagonize replication.
PTM
Sumoylation significantly increases stability. It also promotes interaction specifically with HDAC1 (but not HDAC2, nor HDAC3) and strongly stimulates ESR1 and TP53 coactivation.
Acetylation at lysine residues stabilizes the protein, stimulates interaction with HDAC1 and HDAC3, but not HDAC2, and represses ESR1 and TP53 coactivation activity.

Fortuna, T. R., Kour, S., Anderson, E. N., Ward, C., Rajasundaram, D., Donnelly, C. J., ... & Pandey, U. B. (2021). DDX17 is involved in DNA damage repair and modifies FUS toxicity in an RGG-domain dependent manner. Acta Neuropathologica, 142(3), 515-536.

Mao, R., Dong, M., Shen, Z., Zhang, H., Liu, Y., Cai, D., ... & Guo, H. (2021). RNA Helicase DDX17 Inhibits Hepatitis B Virus Replication by Blocking Viral Pregenomic RNA Encapsidation. Journal of Virology, 95(19), e00444-21.

Luo, Q., Que, T., Luo, H., Meng, Y., Chen, X., Huang, H., ... & Huang, G. (2020). Upregulation of DEAD box helicase 5 and 17 are correlated with the progression and poor prognosis in gliomas. Pathology-Research and Practice, 216(3), 152828.

Nelson, C. R., Mrozowich, T., Park, S. M., D’souza, S., Henrickson, A., Vigar, J. R., ... & Patel, T. R. (2020). Human DDX17 unwinds rift valley fever virus non-coding RNAs. International journal of molecular sciences, 22(1), 54.

Chapus, F. (2020). Role of the DEAD-box Helicases DDX5 and DDX17 in Hepatitis B Virus RNA processing (Doctoral dissertation, Université de Lyon).

Wu, C. Y., & Nagy, P. D. (2019). Blocking tombusvirus replication through the antiviral functions of DDX17-like RH30 DEAD-box helicase. PLoS pathogens, 15(5), e1007771.

Xue, Y., Jia, X., Li, C., Zhang, K., Li, L., Wu, J., ... & Li, Q. (2019). DDX17 promotes hepatocellular carcinoma progression via inhibiting Klf4 transcriptional activity. Cell death & disease, 10(11), 1-11.

Ngo, T. D., Partin, A. C., & Nam, Y. (2019). RNA specificity and autoregulation of DDX17, a modulator of microRNA biogenesis. Cell reports, 29(12), 4024-4035.

Giraud, G., Terrone, S., & Bourgeois, C. F. (2018). Functions of DEAD box RNA helicases DDX5 and DDX17 in chromatin organization and transcriptional regulation. BMB reports, 51(12), 613.

Ask a question We look forward to hearing from you.
0 reviews or Q&As
Loading...
Have you used Mouse Anti-DDX17 Recombinant Antibody (1B5B09)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

Online Inquiry

Documents

Contact us

  • Tel: (USA)
  • (UK)
  • Fax:
  • Email:

Submit A Review

Go to
Compare