COP1 (RFWD2) (NM_022457) Human Mass Spec Standard

CAT#: PH310492

RFWD2 MS Standard C13 and N15-labeled recombinant protein (NP_071902)



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CNY 14,250.00


货期*
5周

规格
    • 10 ug

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Specifications

Product Data
Description RFWD2 MS Standard C13 and N15-labeled recombinant protein (NP_071902)
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC210492
Predicted MW 80.5 kDa
Protein Sequence
Tag C-Myc/DDK
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration >0.05 µg/µL as determined by microplate BCA method
Labeling Method Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Buffer 25 mM Tris-HCl, 100 mM glycine, pH 7.3
Reference Data
RefSeq NP_071902
RefSeq Size 2806
RefSeq ORF 2193
Synonyms CFAP78; FAP78; RFWD2; RNF200
Locus ID 64326
Cytogenetics 1q25.1-q25.2
Summary 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).[UniProtKB/Swiss-Prot Function]
Protein Pathways p53 signaling pathway, Ubiquitin mediated proteolysis
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