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Rabbit Anti-OTUD5 Recombinant Antibody (D8Y2U) (CBMAB-CP1813-LY)

The product is antibody recognizes OTUD5. The antibody D8Y2U immunoassay techniques such as: WB,IP.
See all OTUD5 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Rat, Monkey, Cattle, Dog, Pig
Clone
D8Y2U
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human OTUD5 protein.
Specificity
Human, Rat, Monkey, Cattle, Dog, Pig
Antibody Isotype
IgG
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
Buffer
100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
OTU Deubiquitinase 5
Introduction
This gene encodes a member of the OTU (ovarian tumor) domain-containing cysteine protease superfamily. The OTU domain confers deubiquitinase activity and the encoded protein has been shown to suppress the type I interferon-dependent innate immune response by cleaving the polyubiquitin chain from an essential type I interferon adaptor protein. Cleavage results in disassociation of the adaptor protein from a downstream signaling complex and disruption of the type I interferon signaling cascade. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Oct 2008]
Entrez Gene ID
Human55593
Rat363452
Monkey711927
Cattle539145
Dog480911
Pig100624053
UniProt ID
HumanQ96G74
RatQ2YDU3
MonkeyA0A1D5QBJ6
CattleE1BFW9
DogF1P8I6
PigI3L773
Alternative Names
OTU Deubiquitinase 5; Deubiquitinating Enzyme A; OTU Domain Containing 5; DUBA; OTU Domain-Containing Protein 5; Deubiquinating Enzyme A; EC 3.4.19.12;
Function
Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). Controls neuroectodermal differentiation through cleaving 'Lys-48'-linked ubiquitin chains to counteract degradation of select chromatin regulators such as ARID1A, HDAC2 and HCF1 (PubMed:33523931).
Biological Process
Negative regulation of canonical Wnt signaling pathwayManual Assertion Based On ExperimentIMP:FlyBase
Negative regulation of type I interferon productionTAS:Reactome
Neural crest cell differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of TORC1 signalingManual Assertion Based On ExperimentIMP:FlyBase
Positive regulation of TORC2 signalingManual Assertion Based On ExperimentIMP:FlyBase
Protein deubiquitinationManual Assertion Based On ExperimentIDA:MGI
Protein K48-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Protein K63-linked deubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Response to lipopolysaccharideManual Assertion Based On ExperimentIDA:UniProtKB
Cellular Location
Nucleus
Involvement in disease
Multiple congenital anomalies-neurodevelopmental syndrome, X-linked (MCAND):
An X-linked recessive, congenital disorder characterized by central nervous system, craniofacial, cardiac, skeletal, and genitourinary anomalies. Clinical features include poor growth, short stature, global developmental delay, impaired intellectual development, microcephaly, hydrocephalus, hypotonia, congenital heart defects, hypospadias, and other variable abnormalities. Brain imaging typically shows ventriculomegaly and thin corpus callosum. The severity of the disorder is highly variable, ranging from death in early infancy to survival into the second or third decade.
PTM
Phosphorylation at Ser-177 is required for deubiquitinating activity.

Fu, L., Lu, K., Jiao, Q., Chen, X., & Jia, F. (2023). The Regulation and Double-Edged Roles of the Deubiquitinase OTUD5. Cells, 12(8), 1161.

Hou, T., Dan, W., Liu, T., Liu, B., Wei, Y., Yue, C., ... & Li, L. (2022). Deubiquitinase OTUD5 modulates mTORC1 signaling to promote bladder cancer progression. Cell Death & Disease, 13(9), 778.

Dinallo, V., Di Fusco, D., Di Grazia, A., Laudisi, F., Troncone, E., Di Maggio, G., ... & Monteleone, G. (2022). The deubiquitinating enzyme OTUD5 sustains inflammatory cytokine response in inflammatory bowel disease. Journal of Crohn's and Colitis, 16(1), 122-132.

Cho, J. H., Kim, K., Kim, S. A., Park, S., Park, B. O., Kim, J. H., ... & Kim, S. (2021). Deubiquitinase OTUD5 is a positive regulator of mTORC1 and mTORC2 signaling pathways. Cell Death & Differentiation, 28(3), 900-914.

Guo, Y., Jiang, F., Kong, L., Wu, H., Zhang, H., Chen, X., ... & Gao, C. (2021). OTUD5 promotes innate antiviral and antitumor immunity through deubiquitinating and stabilizing STING. Cellular & molecular immunology, 18(8), 1945-1955.

Beck, D. B., Basar, M. A., Asmar, A. J., Thompson, J. J., Oda, H., Uehara, D. T., ... & Werner, A. (2021). Linkage-specific deubiquitylation by OTUD5 defines an embryonic pathway intolerant to genomic variation. Science advances, 7(4), eabe2116.

Bai, M., Che, Y., Lu, K., & Fu, L. (2020). Analysis of deubiquitinase OTUD5 as a biomarker and therapeutic target for cervical cancer by bioinformatic analysis. PeerJ, 8, e9146.

Li, F., Sun, Q., Liu, K., Zhang, L., Lin, N., You, K., ... & Zhao, W. (2020). OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity. Nature Communications, 11(1), 4184.

De Vivo, A., Sanchez, A., Yegres, J., Kim, J., Emly, S., & Kee, Y. (2019). The OTUD5–UBR5 complex regulates FACT-mediated transcription at damaged chromatin. Nucleic acids research, 47(2), 729-746.

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

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