Anti-COP1 (Rabbit) Antibody （抗COP1兔多克隆抗体）

        COP1 antibody, rabbit polyclonal

Background

Constitutive photomorphogenesis protein 1 (COP1) is an E3 ubiquitin-protein ligase that acts as a repressor of

photomorphogenesis and as an activator of etiolation in darkness. 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. COP1 represses photomorphogenesis in darkness by mediating ubiquitination and subsequent

proteasomal degradation of light-induced transcription factors such as HY5, HYH and LAF1. Cop1 also

down-regulates MYB21, probably via ubiquitination process. Light stimuli abrogate the repression of

photomorphogenesis, possibly due to its localization to the cytoplasm. COP1 could play a role in switching

between skotomorphogenetic and photomorphogenetic pathways. Represses photomorphogenesis and induces

skotomorphogenesis in the dark. Contains a ring finger zinc-binding motif, a coiled-coil domain, and several

WD-40 repeats, similar to G-beta proteins. The C-terminus has homology to TAFII80, a subunit of the TFIID

component of the RNA polymerase II of Drosophila. Nuclear localization in the dark and cytoplasmic in the light.

The mRNA is cell-to-cell mobile.

Other names:

ARABIDOPSIS THALIANA CONSTITUTIVE PHOTOMORPHOGENIC 1, ATCOP1, CONSTITUTIVE

PHOTOMORPHOGENIC 1, COP1, DEETIOLATED MUTANT 340, DET340, EMB168, EMBRYO

DEFECTIVE 168, FUS1, FUSCA 1 AT2G32950

Immunogen: Recombinant protein

Concentration: 1.0mg/ml

Tested applications: Western blot (WB), IF

Expected/apparent MW: 76/82 kDa

Species specificity: Arabidopsis thaliana

Recommended dilution: 1 : 500-2000 (WB, detect endogenous protein ), 1: 100 - 1: 500(optimal dilutions should

be determined by the end use.)

Storage Buffer: PBS Buffer, pH7.4

Storage: Store at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Stable for 2

years from date of receipt. Aliquot to avoid repeated freezing and thawing.