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Mouse Anti-CUL2 Recombinant Antibody (4/CUL-2) (CBMAB-C6431-LY)

This product is antibody recognizes CUL2. The antibody 4/CUL-2 immunoassay techniques such as: WB, IF.
See all CUL2 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Dog, Mouse, Rat
Clone
4/CUL-2
Antibody Isotype
IgG1
Application
WB, IF

Basic Information

Immunogen
Human CUL-2 aa. 18-182
Specificity
Human, Dog, Mouse, Rat
Antibody Isotype
IgG1
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
Concentration
0.25 mg/ml
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
cullin 2
Introduction
CUL2 (Cullin 2) is a Protein Coding gene. Diseases associated with CUL2 include Hypoxia and Von Hippel-Lindau Syndrome. Among its related pathways are Innate Immune System and ErbB signaling pathway. Gene Ontology (GO) annotations related to this gene include ubiquitin protein ligase binding and protein complex binding. An important paralog of this gene is CUL1.
Entrez Gene ID
Human8453
Mouse71745
Rat361258
Dog477952
UniProt ID
HumanQ13617
MouseQ9D4H8
RatD4A0H4
DogE2QRU7
Alternative Names
Cullin 2; CUL-2; Testis Secretory Sperm-Binding Protein Li 238E; Cullin-2;
Function
Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346).

May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF).
Biological Process
G1/S transition of mitotic cell cycle Source: ProtInc
Intrinsic apoptotic signaling pathway Source: ProtInc
Post-translational protein modification Source: Reactome
Protein ubiquitination Source: GO_Central
Regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
Viral process Source: UniProtKB-KW
Cellular Location
Cytosol; Nucleoplasm; Cul2-RING ubiquitin ligase complex; Cullin-RING ubiquitin ligase complex; SCF ubiquitin ligase complex; VCB complex
PTM
Neddylated; which enhances the ubiquitination activity of ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes. CBC(VHL) complex formation seems to promote neddylation. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity).

Diaz, S., Li, L., Wang, K., & Liu, X. (2021). Expression and purification of functional recombinant CUL2• RBX1 from E. coli. Scientific reports, 11(1), 1-10.

Chu, D., Liu, T., Yao, Y., & Luan, N. (2021). LINC00997/MicroRNA 574-3p/CUL2 Promotes Cervical Cancer Development via Mitogen-Activated Protein Kinase Signaling. Molecular and Cellular Biology, 41(8), e00059-21.

Ji, Z., Wang, X., Liu, Y., Zhong, M., Sun, J., & Shang, J. (2021). MicroRNA-574-3p Regulates HIF-α Isoforms Promoting Gastric Cancer Epithelial-Mesenchymal Transition via Targeting CUL2. Digestive diseases and sciences, 1-11.

Zhao, W., Liu, Y., Zhang, L., Ding, L., Li, Y., Zhang, H., ... & Hao, M. (2020). MicroRNA-154-5p regulates the HPV16 E7-pRb pathway in Cervical Carcinogenesis by targeting CUL2. Journal of Cancer, 11(18), 5379.

Faull, S. V., Lau, A., Martens, C., Ahdash, Z., Hansen, K., Yebenes, H., ... & Politis, A. (2019). Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome. Nature communications, 10(1), 1-13.

Odon, V., Georgana, I., Holley, J., Morata, J., & Maluquer de Motes, C. (2018). Novel class of viral ankyrin proteins targeting the host E3 ubiquitin ligase Cullin-2. Journal of Virology, 92(23), e01374-18.

Westrich, J. A., Warren, C. J., Klausner, M. J., Guo, K., Liu, C. W., Santiago, M. L., & Pyeon, D. (2018). Human papillomavirus 16 E7 stabilizes APOBEC3A protein by inhibiting cullin 2-dependent protein degradation. Journal of virology, 92(7), e01318-17.

Michail, O., Moris, D., Theocharis, S., & Griniatsos, J. (2018). Cullin-1 and-2 protein expression in colorectal cancer: correlation with clinicopathological variables. in vivo, 32(2), 391-396.

Cardote, T. A., Gadd, M. S., & Ciulli, A. (2017). Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex. Structure, 25(6), 901-911.

Cardote, T. A., & Ciulli, A. (2017). Structure‐Guided Design of Peptides as Tools to Probe the Protein–Protein Interaction between Cullin‐2 and Elongin BC Substrate Adaptor in Cullin RING E3 Ubiquitin Ligases. ChemMedChem, 12(18), 1491-1496.

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

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