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Mouse Anti-COP1 Recombinant Antibody (1E4) (CBMAB-R0472-CN)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
1E4
Antibody Isotype
IgG2b, κ
Application
ELISA, IF, WB

Basic Information

Immunogen
RFWD2 (632 a.a. ~ 731 a.a) partial recombinant protein.
Host Species
Mouse
Specificity
Human, Mouse
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IF(ICC)10 µg/ml

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

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
Batch dependent

Target

Full Name
COP1, E3 Ubiquitin Ligase
Introduction
COP1 (COP1, E3 Ubiquitin Ligase) is a Protein Coding gene. Among its related pathways are CDK-mediated phosphorylation and removal of Cdc6 and Direct p53 effectors. An important paralog of this gene is RBBP4.
Entrez Gene ID
UniProt ID
Human64326
Mouse26374
HumanQ8NHY2
MouseQ9R1A8
Alternative Names
COP1, E3 Ubiquitin Ligase; Constitutive Photomorphogenesis Protein 1 Homolog; RING-Type E3 Ubiquitin Transferase RFWD2; Ring Finger And WD Repeat Domain 2; RING Finger Protein 200; RNF200; RFWD2; Ring Finger And WD Repeat Domain 2, E3 Ubiquitin Protein Ligase;
Function
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable).
Biological Process
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Post-translational protein modification Source: Reactome
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Response to ionizing radiation Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus speckle. In the nucleus, it forms nuclear speckles.
PTM
Autoubiquitinated. MTA1 destabilizes it by promoting its autoubiquitination.
More Infomation

Ponnu, J., & Hoecker, U. (2021). Illuminating the COP1/SPA ubiquitin ligase: fresh insights into its structure and functions during plant photomorphogenesis. Frontiers in Plant Science, 12, 486.

Zahid, S., Basharat, S., Fakhar, M., & Rashid, S. (2021). Molecular dynamics and structural analysis of the binding of COP1 E3 ubiquitin ligase to β‐catenin and TRIB pseudokinases. Proteins: Structure, Function, and Bioinformatics.

Ponnu, J. (2020). Molecular mechanisms suppressing COP1/SPA E3 ubiquitin ligase activity in blue light. Physiologia Plantarum, 169(3), 418-429.

Xu, D. (2020). COP1 and BBXs‐HY5‐mediated light signal transduction in plants. New Phytologist, 228(6), 1748-1753.

Blanco-Touriñán, N., Legris, M., Minguet, E. G., Costigliolo-Rojas, C., Nohales, M. A., Iniesto, E., ... & Alabadí, D. (2020). COP1 destabilizes DELLA proteins in Arabidopsis. Proceedings of the National Academy of Sciences, 117(24), 13792-13799.

Newton, K., Dugger, D. L., Sengupta-Ghosh, A., Ferrando, R. E., Chu, F., Tao, J., ... & Dixit, V. M. (2018). Ubiquitin ligase COP1 coordinates transcriptional programs that control cell type specification in the developing mouse brain. Proceedings of the National Academy of Sciences, 115(44), 11244-11249.

Podolec, R., & Ulm, R. (2018). Photoreceptor-mediated regulation of the COP1/SPA E3 ubiquitin ligase. Current Opinion in Plant Biology, 45, 18-25.

Durzynska, I., Xu, X., Adelmant, G., Ficarro, S. B., Marto, J. A., Sliz, P., ... & Blacklow, S. C. (2017). STK40 is a pseudokinase that binds the E3 ubiquitin ligase COP1. Structure, 25(2), 287-294.

Hoecker, U. (2017). The activities of the E3 ubiquitin ligase COP1/SPA, a key repressor in light signaling. Current opinion in plant biology, 37, 63-69.

Balcerowicz, M., Kerner, K., Schenkel, C., & Hoecker, U. (2017). SPA proteins affect the subcellular localization of COP1 in the COP1/SPA ubiquitin ligase complex during photomorphogenesis. Plant Physiology, 174(3), 1314-1321.

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

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