RFWD2 Blocking Peptide (C-term)
€363.00
In stock
SKU
AC-BP19933b
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.
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
Gene Name: COP1 (HGNC:17440)
Gene ID: 64326
Primary Accession: Q8NHY2
Other Accession: Q9R1A8; NP_071902.2
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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.
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
Gene Name: COP1 (HGNC:17440)
Gene ID: 64326
Primary Accession: Q8NHY2
Other Accession: Q9R1A8; NP_071902.2
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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