Beta catenin; Beta-catenin; Cadherin associated protein; Catenin (cadherin associated protein), beta 1, 88kDa; Catenin beta 1; Catenin beta-1; CATNB; CHBCAT; CTNB1_HUMAN; CTNNB; CTNNB1; DKFZp686D02253; FLJ25606; FLJ37923; OTTHUMP00000162082; OTTHUMP00000165222; OTTHUMP00000165223; OTTHUMP00000209288; OTTHUMP00000209289;
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:200, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
beta Catenin Antibody detects endogenous levels of total beta Catenin.
1mg/ml in PBS, pH 7.4.
A synthesized peptide derived from human beta Catenin, corresponding to a region within N-terminal amino acids.
Observed Mol.Wt.: 92kDa.
Predicted Mol.Wt.: 86kDa.
Cytoplasm. Nucleus. Cytoplasm > cytoskeleton. Cell junction > adherens junction. Cell junction. Cell membrane. 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.
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). Expressed in breast cancer tissues (at protein level) (PubMed:29367600).
Beta-catenin is an adherens junction protein. Adherens junctions (AJs; also called the zonula adherens) are critical for the establishment and maintenance of epithelial layers, such as those lining organ surfaces. AJs mediate adhesion between cells, communicate a signal that neighboring cells are present, and anchor the actin cytoskeleton. In serving these roles, AJs regulate normal cell growth and behavior.
10 20 30 40 50
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG
60 70 80 90 100
NPEEEDVDTS QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP
110 120 130 140 150
ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT
160 170 180 190 200
RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR
210 220 230 240 250
TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS
260 270 280 290 300
VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
310 320 330 340 350
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC
360 370 380 390 400
SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG
410 420 430 440 450
LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT
460 470 480 490 500
VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP
510 520 530 540 550
PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR
560 570 580 590 600
TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
610 620 630 640 650
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG
660 670 680 690 700
VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI
710 720 730 740 750
GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV
760 770 780
DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L
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, as component of an E-cadherin:catenin adhesion complex. 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).
Phosphorylation at Ser-552 by AMPK promotes stabilizion of the protein, enhancing TCF/LEF-mediated transcription (By similarity). Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-37 and Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding and enhances TBP binding. Phosphorylated on Ser-33 and Ser-37 by HIPK2 and GSK3B, this phosphorylation triggers proteasomal degradation (PubMed:25169422). Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity.Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity).S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions.O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1.Deacetylated at Lys-49 by SIRT1.
Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin:catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Another cytoplasmic pool is part of a large complex containing 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. Wnt-dependent activation of DVL antagonizes the action of GSK3B. When GSK3B activity is inhibited the complex dissociates, CTNNB1 is dephosphorylated and is no longer targeted for destruction. The stabilized protein translocates to the nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9, BCL9L and possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3, CXADR and PCDH11Y. Binds SLC9A3R1. Interacts with GLIS2 and MUC1. Interacts with SLC30A9. Interacts with XIRP1. Interacts directly with AXIN1; the interaction is regulated by CDK2 phosphorylation of AXIN1. Interacts with SCRIB. Interacts with RAPGEF2. Interacts with PTPRU (via the cytoplasmic juxtamembrane domain). Interacts with EMD. Interacts with TNIK and TCF7L2. Interacts with SESTD1 and TRPC4. Interacts with CAV1. Interacts with TRPV4. The TRPV4 and CTNNB1 complex can interact with CDH1. Interacts with VCL. Interacts with PTPRJ. Interacts with PKT7 and CDK2. Interacts with FAT1 (via the cytoplasmic domain). Interacts with NANOS1 and NDRG2. Interacts with isoform 1 of NEK2. Interacts with both isoform 1 and isoform 2 of CDK5. Interacts with PTK6. Interacts with SOX7; this interaction may lead to proteasomal degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin-stimulated transcription. Identified in a complex with HINT1 and MITF. Interacts with FHIT. The CTNNB1 and TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Interacts with FERMT2. Identified in a complex with TCF7L2/TCF4 and FERMT2. Interacts with RORA. May interact with P-cadherin/CDH3. Interacts with RNF220 (PubMed:25266658). Interacts with CTNND2 (PubMed:25807484). Interacts (via the C-terminal region) with CBY1 (PubMed:12712206, PubMed:16424001). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (PubMed:25169422). Interacts with DLG5 (By similarity). Interacts with FAM53B; promoting translocation to the nucleus (PubMed:25183871). Interacts with TMEM170B (PubMed:29367600). Interacts with AHI1 (PubMed:21623382).
Belongs to the beta-catenin family.
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Adherens junction.(View pathway)
· Cellular Processes > Cellular community - eukaryotes > Signaling pathways regulating pluripotency of stem cells.(View pathway)
· Environmental Information Processing > Signal transduction > Hippo signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Wnt signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.(View pathway)
· Human Diseases > Cancers: Specific types > Basal cell carcinoma.(View pathway)
· Human Diseases > Cancers: Specific types > Thyroid cancer.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Gastric cancer.(View pathway)
· Human Diseases > Cancers: Specific types > Colorectal cancer.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.(View pathway)
· Human Diseases > Cancers: Specific types > Endometrial cancer.(View pathway)
· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).
· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.
· Human Diseases > Cancers: Specific types > Breast cancer.(View pathway)
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Human Diseases > Infectious diseases: Viral > HTLV-I infection.
· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.
· Human Diseases > Cancers: Specific types > Prostate cancer.(View pathway)
· Organismal Systems > Immune system > Leukocyte transendothelial migration.(View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.(View pathway)
· Organismal Systems > Endocrine system > Melanogenesis.
Application: WB Species:human; Sample:Not available
Figure 4 miR-200c decreases α1,3-fucosylation on CD44 and inactivates Wnt/β-catenin signaling pathway. (a, e) Western/lectin blot analysis of effect of miR-200c on α1,3- fucosylation and LeY biosynthesis in RL95-2 (a) and Ishikawa (e) cells. CBB: coomassie brilliant blue. LTL: Lotus tetragonolobus lectin. (b, f) Immunoprecipitation and western blot analysis of α 1,3-fucosylation and LeY on CD44 in RL95-2 (b) and Ishikawa (f) cells. Immunoprecipitation (IP): anti-CD44 antibody pulled down protein. Immune blot (IB): detection of α 1,3-fucosylation by LTL lectin and anti-LeY antibody. (c, g) Western blot analysis of CD44, LTL and LeY blocking on activation of p-GSK3β, GSK3β and β-catenin in RL95-2 (c) and Ishikawa (g) cells. (d, h) Western blot and statistical analysis of p-GSK3β, GSK3β and β-catenin in RL95-2 (d) and Ishikawa (h) cells. DKK: inhibitor of Wnt/β- catenin signal pathway. *Po0.05, **Po0.01, ***Po0.
Application: WB Species:human; Sample:Not available
Figure 2 The expression of epithelial –mesenchymal transition (EMT) markers and b-catenin was detected at each time point. (A) Immunoblotting analysis of human primary cultured endometrial epithelial cell extracts using the corresponding antibodies. The ratios of each protein relative to non-treated cells were normalized to GAPDH. (B) The relative expression of HIF-1a, N-cadherin, E-cadherin, b-catenin, vimentin and snail proteins in human endometrial epithelial glands under hypoxic conditions at each time point was investigated by western blot. Data are represented as mean+SD and are representative of the relative expression of protein normalized by GAPDH. All experiments were repeated four times. Data were evaluated by one-way ANOVA analysis (*P , 0.05, **P , 0.01 compared with untreated group). (C) The changed cellular morphologies of human endometrial epithelial glands in hypoxia compared with cells in normoxia, the hypoxic time was 48 h. Red arrows indicate the spindle-shaped and fibroblast-like cells.
Application: IHC Species:human; Sample:Not available
Figure 1 EMT occurs in endometrial epithelial cells of ovarian endometriosis samples. Representative photomicrographs of HIF-1a (A–C), b-catenin (D–F), E-cadherin (G–I), N-cadherin (J–L) and vimentin (M–O) in normal endometrium (A, D, G, J, M), eutopic endometrium (B, E, H, K, N) and ovarian endometriosis (C, F, I, L,O). (P)Colon cancer tissue that was positive for HIF-1a. (Q) Healthy liver tissue that was negative for HIF-1a. (R) Peptide-blocking reagent without antibody was applied as the negative controls. Photographs were taken at magnifications of ×200 (left panels) and ×400 (right panels). N, normal endometrium; U, eutopic endometrium; E, ovarian endometriosis.
Application: WB Species:human; Sample:A549 cells
Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|S29||Phosphorylation||P68400 (CSNK2A1) , P67870 (CSNK2B) , P19784 (CSNK2A2)||Uniprot|
|S33||Phosphorylation||O15111 (CHUK) , P49841 (GSK3B) , P45983 (MAPK8) , Q9H2X6 (HIPK2) , P49840 (GSK3A)||Uniprot|
|S37||Phosphorylation||P49840 (GSK3A) , P45983 (MAPK8) , P49841 (GSK3B) , O15111 (CHUK) , Q9H2X6 (HIPK2)||Uniprot|
|T41||Phosphorylation||P49840 (GSK3A) , P45983 (MAPK8) , O15111 (CHUK) , P49841 (GSK3B)||Uniprot|
|S45||Phosphorylation||O15111 (CHUK) , P48730 (CSNK1D) , P17612 (PRKACA) , P48729 (CSNK1A1) , P49674 (CSNK1E) , Q8N752 (CSNK1A1L) , Q00534 (CDK6) , Q05513 (PRKCZ)||Uniprot|
|Y86||Phosphorylation||P00519 (ABL1) , P12931 (SRC)||Uniprot|
|T102||Phosphorylation||P68400 (CSNK2A1) , P19784 (CSNK2A2) , P67870 (CSNK2B)||Uniprot|
|T112||Phosphorylation||Q15139 (PRKD1) , P67870 (CSNK2B) , P19784 (CSNK2A2) , P68400 (CSNK2A1)||Uniprot|
|Y142||Phosphorylation||P04629 (NTRK1) , Q13882 (PTK6) , P21802 (FGFR2) , P22607 (FGFR3) , P06241 (FYN) , P16591 (FER) , P00533 (EGFR)||Uniprot|
|S191||Phosphorylation||P45984 (MAPK9) , Q00535 (CDK5)||Uniprot|
|T332||Phosphorylation||Q9UQM7 (CAMK2A) , Q13554 (CAMK2B)||Uniprot|
|Y333||Phosphorylation||P12931 (SRC) , Q13882 (PTK6)||Uniprot|
|T472||Phosphorylation||Q13554 (CAMK2B) , Q9UQM7 (CAMK2A)||Uniprot|
|S552||Phosphorylation||Q9UQM7 (CAMK2A) , P17612 (PRKACA) , P54646 (PRKAA2) , P31751 (AKT2) , Q13554 (CAMK2B) , P31749 (AKT1)||Uniprot|
|S605||Phosphorylation||P53778 (MAPK12) , P45984 (MAPK9)||Uniprot|
|Y654||Phosphorylation||P07949 (RET) , P04626 (ERBB2) , P00533 (EGFR) , P00519 (ABL1) , P36888 (FLT3) , P12931 (SRC)||Uniprot|
|S675||Phosphorylation||O96013 (PAK4) , Q13153 (PAK1) , P17612 (PRKACA)||Uniprot|