The cellular level of β-catenin is mostly controlled by its ubiquitination and proteosomal degradation. The E3 ubiquitin ligase TrCP1 (also known as β-TrCP) can recognize β-catenin as its substrate through a short linear motif on the disordered N-terminus. However, this motif (Asp-Ser-Gly-Ile-His-Ser) of β-catenin needs to be phosphorylated on the two serines in order to be capable to bind β-TrCP. Phosphorylation of the motif is performed by Glycogen Synthase Kinase 3 alpha and beta (GSK3α and GSK3β). GSK3s are constitutively active enzymes implicated in several important regulatory processes. There is one requirement, though: substrates of GSK3 need to be pre-phosphorylated four amino acids downstream (C-terminally) of the actual target site. Thus it also requires a "priming kinase" for its activities. In the case of β-catenin, the most important priming kinase is Casein Kinase I (CKI). Once a serine-threonine rich substrate has been "primed", GSK3 can "walk" across it from C-terminal to N-terminal direction, phosphorylating every 4th serine or threonine residues in a row. This process will result in dual phosphorylation of the aforementioned β-TrCP recognition motif as well.

Catenin beta-1
Beta-catenin
CTNNB1
CTNNB

p35222

WB,IHC,IF,ICC,FC

WB 1:2000
IHC 1:200
IF 1:100-1:400
ICC 1:100
FC 1:1000

Human,Mouse,Rat

Predicted size: 85 kDa

Rabbit

Cytoplasm, Nucleus, Cell membrane.

Protein A affinity purified.

Recombinant Rabbit monoclonal

IgG

Liquid

PBS (pH7.4), 0.1% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.