Human Recombinant NEDD8 protein, His Tag (V2LY-0526-LY5730)

Name: Human Recombinant NEDD8 protein, His Tag
SKU: V2LY-0526-LY5730
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

E. coli

Protein Species

Human

Tag

His Tag

Protein Construction

This product is Human Recombinant NEDD8 protein, His Tag consist of Amino Acid: 1-76 and predicts a molecular mass of 10 kDa.

Molecule Mass

10 kDa

Sequence

Amino Acid: 1-76

Species

Human

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

Purity

Batch dependent.

Endotoxin

Please contact us for more information.

Format

Liquid

Buffer

PBS

Preservative

None

Storage

Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

More Infomation

Target

Full Name

Neural Precursor Cell Expressed, Developmentally Down-Regulated 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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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