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Mouse Anti-ILF3 Recombinant Antibody (21/DRBP76) (CBMAB-D2090-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Interleukin Enhancer Binding Factor 3 (ILF3). The antibody can be used for immunoassay techniques, such as WB, IF.
See all ILF3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
21/DRBP76
Antibody Isotype
IgG1
Application
WB, IF

Basic Information

Immunogen
Human DRBP76 a.a.592-695
Specificity
Human
Antibody Isotype
IgG1
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
interleukin enhancer binding factor 3
Introduction
ILF3 is a double-stranded RNA (dsRNA) binding protein that complexes with other proteins, dsRNAs, small noncoding RNAs, and mRNAs to regulate gene expression and stabilize mRNAs. This protein (NF90, ILF3) forms a heterodimer with a 45 kDa transcription factor (NF45, ILF2) required for T-cell expression of interleukin 2. This complex has been shown to affect the redistribution of nuclear mRNA to the cytoplasm. Knockdown of NF45 or NF90 protein retards cell growth, possibly by inhibition of mRNA stabilization. In contrast, an isoform (NF110) of this gene that is predominantly restricted to the nucleus has only minor effects on cell growth when its levels are reduced.
Entrez Gene ID
3609
UniProt ID
Q12906
Alternative Names
Interleukin Enhancer Binding Factor 3
Function
RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs (PubMed:28625552).
As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398).
Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response (PubMed:21123651, PubMed:34110282).
Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs (PubMed:21123651, PubMed:28625552).
(Microbial infection) Plays a positive role in HIV-1 virus production by binding to and thereby stabilizing HIV-1 RNA, together with ILF3.
Biological Process
Defense response to virusIEA:UniProtKB-KW
Negative regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of translationISS:UniProtKB
Negative regulation of viral genome replicationISS:UniProtKB
Positive regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Cellular Location
Nucleus, nucleolus; Cytoplasm; Nucleus. Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
PTM
Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication.
Methylated by protein arginine N-methyltransferase 1.
Ubiquitinated at Lys-297 in a TRIM47-dependent manner; this 'Lys-48'-linked ubiquitination promotes ILF3 degradation.

Qiu, J., Wu, X., Luo, Y., Yao, Y., Zhang, X., Pan, B., ... & Tang, N. (2023). Prognostic and immunotherapeutic predictive value of interleukin enhancer-binding factor 3 in hepatocellular carcinoma: Integrated bioinformatics and experimental analysis. Gene, 856, 147132.

Li, P., Mi, Q., Yan, S., Xie, Y., Cui, Z., Zhang, S., ... & Wang, C. (2023). Characterization of circSCL38A1 as a novel oncogene in bladder cancer via targeting ILF3/TGF-β2 signaling axis. Cell Death & Disease, 14(1), 59.

Huang, Y., Zheng, Y., Yao, L., Qiao, F., Hou, Y., Hu, X., ... & Shao, Z. (2022). RNA binding protein POP7 regulates ILF3 mRNA stability and expression to promote breast cancer progression. Cancer Science, 113(11), 3801-3813.

Xu, Z., Huang, H., Li, X., Ji, C., Liu, Y., Liu, X., ... & Shi, J. (2020). High expression of interleukin‑enhancer binding factor 3 predicts poor prognosis in patients with lung adenocarcinoma. Oncology Letters, 19(3), 2141-2152.

Liu, Y., Li, Y., Zhao, Y., Liu, Y., Fan, L., Jia, N., & Zhao, Q. (2019). ILF3 promotes gastric cancer proliferation and may be used as a prognostic marker. Molecular Medicine Reports, 20(1), 125-134.

Jia, R., Ajiro, M., Yu, L., McCoy, P., & Zheng, Z. M. (2019). Oncogenic splicing factor SRSF3 regulates ILF3 alternative splicing to promote cancer cell proliferation and transformation. Rna, 25(5), 630-644.

Vrakas, C. N., Herman, A. B., Ray, M., Kelemen, S. E., Scalia, R., & Autieri, M. V. (2019). RNA stability protein ILF3 mediates cytokine-induced angiogenesis. The FASEB Journal, 33(3), 3304.

Cheng, C. C., Chou, K. F., Wu, C. W., Su, N. W., Peng, C. L., Su, Y. W., ... & Chang, Y. F. (2018). EGFR-mediated interleukin enhancer-binding factor 3 contributes to formation and survival of cancer stem-like tumorspheres as a therapeutic target against EGFR-positive non-small cell lung cancer. Lung Cancer, 116, 80-89.

Wu, T. H., Shi, L., Adrian, J., Shi, M., Nair, R. V., Snyder, M. P., & Kao, P. N. (2018). NF90/ILF3 is a transcription factor that promotes proliferation over differentiation by hierarchical regulation in K562 erythroleukemia cells. PloS one, 13(3), e0193126.

Cheng, C. C., Chou, K. F., Wu, C. W., Su, N. W., Peng, C. L., Su, Y. W., ... & Chang, Y. F. (2018). EGFR-mediated interleukin enhancer-binding factor 3 contributes to formation and survival of cancer stem-like tumorspheres through regulating HER3/ERBB3 expression as a therapeutic target against EGFR-positive non-small cell lung cancer. Cancer Research, 78(13_Supplement), 3060-3060.

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For research use only. Not intended for any clinical use.

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