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Mouse Anti-OTUD4 (AA 815-1049) Recombinant Antibody (3B12G11) (CBMAB-O0036-CQ)

This product is a mouse antibody that recognizes OTUD4 (AA 815-1049). The antibody 3B12G11 can be used for immunoassay techniques such as: WB, FC, ELISA, IHC, ICC, CyTOF.
See all OTUD4 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Rat
Clone
3B12G11
Application
WB, FC, ELISA, IHC, ICC, CyTOF

Basic Information

Immunogen
Purified recombinant fragment of human OTUD4 (AA: 815-1049) expressed in E. Coli
Specificity
Human, Rat
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!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 815-1049

Target

Full Name
OTU domain containing 4
Introduction
Alternatively spliced transcript variants have been found for this gene. The smaller protein isoform encoded by the shorter transcript variant is found only in HIV-1 infected cells.
Entrez Gene ID
Human54726
Rat307774
UniProt ID
HumanQ01804
RatF1M7Q7
Alternative Names
OTU Deubiquitinase 4; HIN1; OTU Domain-Containing Protein 4; HIV-1 Induced Protein HIN-1; HIV-1-Induced Protein HIN-1; OTU Domain Containing 4
Function
Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein (PubMed:23827681, PubMed:25944111, PubMed:29395066).
May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators (PubMed:29395066).
Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111).
Biological Process
Innate immune responseIEA:UniProtKB-KW
Negative regulation of interleukin-1-mediated signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of toll-like receptor signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of DNA demethylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein deubiquitinationManual Assertion Based On ExperimentIBA:GO_Central
Protein K48-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Protein K63-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of protein K48-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Cellular Location
Cytoplasm
Nucleus
Primarily cytoplasmic.
PTM
Phosphorylated on Ser-202 and Ser-204 likely by CSNK2A1-CSNK2A2 serine/threonine-protein kinase complex. Activates 'Lys-63'-specific deubiquitinase activity.

Hu, S., Yuan, Y., Yan, R., Xie, H., Cai, R., & Xu, J. (2024). NRF2 regulates EGF stability through OTUD4 in lung adenocarcinoma. Biochemical and Biophysical Research Communications, 149798.

Ma, X., Wan, R., Wen, Y., Liu, T., Song, Y., & Zhu, Y. (2024). Deubiquitinating enzyme OTUD4 regulates metastasis in triple-negative breast cancer by stabilizing Snail1. Experimental Cell Research, 434(1), 113864.

Gao, Y., Tang, J., Ma, X., Zhang, C., Huang, L., Che, J., ... & Zhang, H. (2023). OTUD4 regulates metastasis and chemoresistance in melanoma by stabilizing Snail1. Journal of Cellular Physiology, 238(11), 2546-2555.

Yu, K., Guo, Y. Y., Liuyu, T., Wang, P., Zhang, Z. D., Lin, D., & Zhong, B. (2023). The deubiquitinase OTUD4 inhibits the expression of antimicrobial peptides in Paneth cells to support intestinal inflammation and bacterial infection. Cell Insight, 2(3), 100100.

Luo, L., Li, T., Zeng, Z., Li, H., He, X., & Chen, Y. (2023). CSE reduces OTUD4 triggering lung epithelial cell apoptosis via PAI-1 degradation. Cell Death & Disease, 14(9), 614.

Jaynes, P. W., Iyengar, P. V., Lui, S. K. L., Tan, T. Z., Vasilevski, N., Wright, S. C. E., ... & Eichhorn, P. J. A. (2020). OTUD4 enhances TGFβ signalling through regulation of the TGFβ receptor complex. Scientific Reports, 10(1), 15725.

Zhao, X., Su, X., Cao, L., Xie, T., Chen, Q., Li, J., ... & Jiang, C. (2020). OTUD4: A potential prognosis biomarker for multiple human cancers. Cancer Management and Research, 1503-1512.

Liu, H., Fan, J., Zhang, W., Chen, Q., Zhang, Y., & Wu, Z. (2020). OTUD4 alleviates hepatic ischemia-reperfusion injury by suppressing the K63-linked ubiquitination of TRAF6. Biochemical and Biophysical Research Communications, 523(4), 924-930.

Liuyu, T., Yu, K., Ye, L., Zhang, Z., Zhang, M., Ren, Y., ... & Zhong, B. (2019). Induction of OTUD4 by viral infection promotes antiviral responses through deubiquitinating and stabilizing MAVS. Cell Research, 29(1), 67-79.

Das, R., Schwintzer, L., Vinopal, S., Aguado Roca, E., Sylvester, M., Oprisoreanu, A. M., ... & Broemer, M. (2019). New roles for the de-ubiquitylating enzyme OTUD4 in an RNA–protein network and RNA granules. Journal of cell science, 132(12), jcs229252.

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

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