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RFWD2 Blocking Peptide (C-term)

Synthetic peptide

     
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Product Information
Primary Accession Q8NHY2
Other Accession Q9R1A8, NP_071902.2
Additional Information
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 The synthetic peptide sequence is selected from aa 687-701 of HUMAN RFWD2
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RFWD2
Synonyms COP1, RNF200
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.
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
Research Areas
Citations (0)

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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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$ 80.00
Cat# BP19933b
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