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.
RFWD2
Reactivity: Human
WB, ELISA
Host: Rabbit
Polyclonal
unconjugated
Application Notes
For WB starting dilution is: 1:1000
Restrictions
For Research Use only
Format
Liquid
Concentration
0.5 mg/mL
Buffer
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
Storage Comment
Store at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Target
RFWD2
(Ring Finger and WD Repeat Domain 2, E3 Ubiquitin Protein Ligase (RFWD2))
COP1 antibody, RNF200 antibody, AI316802 antibody, C80879 antibody, Cop1 antibody, RGD1304773 antibody, RFWD2 antibody, cop1 antibody, rnf200 antibody, zgc:163067 antibody, ring finger and WD repeat domain 2 antibody, ring finger and WD repeat domain 2, E3 ubiquitin protein ligase antibody, ring finger and WD repeat domain 2, E3 ubiquitin protein ligase L homeolog antibody, RFWD2 antibody, Rfwd2 antibody, rfwd2 antibody, rfwd2.L antibody
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.