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RFWD2 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q8NHY2 |
| Other Accession | Q9R1A8, NP_071902.2 |
| Reactivity | Human |
| Predicted | Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 80474 Da |
| Antigen Region | 672-701 aa |
| Gene ID | 64326 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase RFWD2, 632-, Constitutive photomorphogenesis protein 1 homolog, hCOP1, RING finger and WD repeat domain protein 2, RING finger protein 200, RFWD2, COP1, RNF200 |
| Target/Specificity | This RFWD2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 672-701 amino acids from the C-terminal region of human RFWD2. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | RFWD2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | COP1 (HGNC:17440) |
|---|---|
| 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). |
| Cellular Location | Nucleus speckle. Cytoplasm. Note=In the nucleus, it forms nuclear speckles |
| Tissue Location | Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Kinyo, A., et al. J. Invest. Dermatol. 130(2):541-545(2010)
Li, D.Q., et al. Proc. Natl. Acad. Sci. U.S.A. 106(41):17493-17498(2009)
Kato, S., et al. J. Biol. Chem. 283(51):35464-35473(2008)
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