Cited in 3+ publications.
The Rabbit Polyclonal anti-RFWD2 antibody (Clone RB41831) (ABIN1881747) specifically detects RFWD2 in WB.
The antibody is reactive with Human samples.
This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
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.
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Shimada, Miyagawa, Kawashima, Tanaka, Honda, Honda, Tokunaga: "An approach based on a genome-wide association study reveals candidate loci for narcolepsy." in: Human genetics, Vol. 128, Issue 4, pp. 433-41, (2010) (PubMed).
Li, Ohshiro, Reddy, Pakala, Lee, Zhang, Rayala, Kumar: "E3 ubiquitin ligase COP1 regulates the stability and functions of MTA1." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, Issue 41, pp. 17493-8, (2009) (PubMed).
Kato, Ding, Pisck, Jhala, Du: "COP1 functions as a FoxO1 ubiquitin E3 ligase to regulate FoxO1-mediated gene expression." in: The Journal of biological chemistry, Vol. 283, Issue 51, pp. 35464-73, (2008) (PubMed).
Target
RFWD2
(Ring Finger and WD Repeat Domain 2, E3 Ubiquitin Protein Ligase (RFWD2))
Alternative Name
RFWD2
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.