|Calculated MW||85497 Da|
|Other Names||Catenin beta-1, Beta-catenin, CTNNB1, CTNNB|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding threonine 41 and 45 of human Beta-catenin was used as an immunogen. This antibody detects Beta-catenin phosphorylated on threonine 41 and/or 45.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Beta-Catenin Antibody Phospho (pT41/pT45) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell junction. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1 Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells.|
|Tissue Location||Expressed in several hair follicle cell types: basal and peripheral matrix cells, and cells of the outer and inner root sheaths. Expressed in colon. Present in cortical neurons (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Beta-catenin is a key regulatory protein involved in cell adhesion and signal transduction through the Wnt pathway, and plays important roles in development, cellular proliferation, and differentiation (1). Beta-catenin is phosphorylated at four serine and threonine residues at the N-terminus (2). Ser 45 is phosphorylated by CK1, and is thought to be a priming site for the phosphorylation by glycogen synthase kinase-3 (GSK-3) of the remaining three residues, Thr 41, Ser 37, and Ser 33 (2). Wnt signaling antagonizes the action of GSK-3, which in subsequent phosphorylation steps, leads to its degradation (3). Mutations in the Beta-catenin gene, CTNNB1, have been implicated in its accumulation and various forms of carcinomas (4).
1. Kikuchi, et al. Biochem Biophys Res Commun. 268: 243-8 (2000).
2. Hagen, T., et al. Biochem Biophys Res Commun. 294: 324-8 (2002).
3. van Noort, M., et al. J Biol Chem. 277: 17901-5 (2002).
4. Blaker, H., et al. Genes Chromosomes Cancer. 25: 399-402 (1999).
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