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Rabbit Anti-NEDD8 Recombinant Antibody (Y297) (CBMAB-N0222-WJ)

This product is a Rabbit antibody that recognizes NEDD8. The antibody Y297 can be used for immunoassay techniques such as: WB, IP, IHC-P, ICC.
See all NEDD8 antibodies
Published Data
Fig.1 Western blot analysis of NEDD8 expression in HeLa or HEK293T cells transfected with scramble siRNA, NEDD8 siRNA 1, NEDD8 siRNA 2, or NEDD8 siRNA 3 for 48 h.
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Summary

Host Animal
Rabbit
Specificity
Rat, Human
Clone
Y297
Antibody Isotype
IgG
Application
WB, IP, IHC-P, ICC

Basic Information

Specificity
Rat, Human
Antibody Isotype
IgG
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
Neural Precursor Cell Expressed, Developmentally Down-Regulated 8
Introduction
Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.
Entrez Gene ID
Human4738
Rat25490
UniProt ID
HumanQ15843
RatQ71UE8
Alternative Names
Neural Precursor Cell Expressed, Developmentally Down-Regulated 8; Ubiquitin-Like Protein Nedd8; Neddylin; NEDD-8; Neural Precursor Cell Expressed Developmentally Down-Regulated Protein 8;
Function
Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53 (PubMed:9694792, PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:15242646, PubMed:14690597).

Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins (PubMed:9694792, PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:20688984).

Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity (PubMed:15242646).

Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M (PubMed:14690597).
Biological Process
Anatomical structure morphogenesis Source: ProtInc
Cellular protein modification process Source: ProtInc
Modification-dependent protein catabolic process Source: GO_Central
Protein localization Source: Ensembl
Protein neddylation Source: MGI
Proteolysis Source: ProtInc
Regulation of proteolysis Source: GO_Central
Regulation of transcription by RNA polymerase II Source: Ensembl
Ubiquitin-dependent protein catabolic process Source: ProtInc
Cellular Location
Nucleus
Note: Mainly nuclear.
PTM
Cleavage of precursor form by UCHL3 or SENP8 is necessary for function.
(Microbial infection) Deamidated at Gln-40 by bacterial cyclomodulin Cif produced by enteropathogenic E.coli, Y.pseudotuberculosis or B.pseudomallei, leading to impair NEDD8 ability to activate cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes) (PubMed:20688984, PubMed:21903097, PubMed:23589306, PubMed:26632597, PubMed:23175788). Deamidation occurs on NEDD8-modified cullins (PubMed:20850415, PubMed:21903097). NEDD8 deamidation prevents switching from the inactive to active state by maintaining the 'closed' structure of the CRL complexes (PubMed:23589306, PubMed:26632597). Deamidation may also impair its deconjugation by the COP9 signalosome; However this result needs additional evidences (PubMed:20850415, PubMed:21903097).

Fu, D. J., & Wang, T. (2023). Targeting NEDD8-activating enzyme for cancer therapy: developments, clinical trials, challenges and future research directions. Journal of Hematology & Oncology, 16(1), 87.

Zhou, L., Lin, X., Zhu, J., Zhang, L., Chen, S., Yang, H., ... & Chen, B. (2023). NEDD8-conjugating enzyme E2s: Critical targets for cancer therapy. Cell Death Discovery, 9(1), 23.

Kostrhon, S., Prabu, J. R., Baek, K., Horn-Ghetko, D., von Gronau, S., Kluegel, M., ... & Schulman, B. A. (2021). CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation. Nature chemical biology, 17(10), 1075-1083.

Stuber, K., Schneider, T., Werner, J., Kovermann, M., Marx, A., & Scheffner, M. (2021). Structural and functional consequences of NEDD8 phosphorylation. Nature Communications, 12(1), 5939.

Baek, K., Scott, D. C., & Schulman, B. A. (2021). NEDD8 and ubiquitin ligation by cullin-RING E3 ligases. Current opinion in structural biology, 67, 101-109.

Santonico, E. (2020). Old and new concepts in ubiquitin and NEDD8 recognition. Biomolecules, 10(4), 566.

Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L. M., ... & Schulman, B. A. (2020). NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly. Nature, 578(7795), 461-466.

Keuss, M. J., Hjerpe, R., Hsia, O., Gourlay, R., Burchmore, R., Trost, M., & Kurz, T. (2019). Unanchored tri‐NEDD8 inhibits PARP‐1 to protect from oxidative stress‐induced cell death. The EMBO Journal, 38(6), e100024.

Li, L., Kang, J., Zhang, W., Cai, L., Wang, S., Liang, Y., ... & Jia, L. (2019). Validation of NEDD8-conjugating enzyme UBC12 as a new therapeutic target in lung cancer. EBioMedicine, 45, 81-91.

Bailly, A. P., Perrin, A., Serrano-Macia, M., Maghames, C., Leidecker, O., Trauchessec, H., ... & Xirodimas, D. P. (2019). The balance between mono-and NEDD8-chains controlled by NEDP1 upon DNA damage is a regulatory module of the HSP70 ATPase activity. Cell Reports, 29(1), 212-224.

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

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