Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000, IF/ICC 1:200-1:1000, FCM 1:200-1:400
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFB1481]
Specificity:
CTNNB1 antibody detects endogenous levels of total CTNNB1.
RRID:
AB_2833506
Cite Format: Affinity Biosciences Cat# BF0319, RRID:AB_2833506.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:

Purified recombinant fragment of human CTNNB1 expressed in E. Coli.

Uniprot:
Gene(ID):
Expression:
P35222 CTNB1_HUMAN:

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).

Description:
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. At several stages of embryogenesis, wound healing, and tumor cell metastasis, cells form and leave epithelia. This process, which involves the disruption and reestablishment of epithelial cell-cell contacts, may be regulated by the disassembly and assembly of AJs. AJs may also function in the transmission of the 'contact inhibition' signal, which instructs cells to stop dividing once an epithelial sheet is complete
Sequence:
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL

PTMs - P35222 As Substrate

Site PTM Type Enzyme
A2 Acetylation
K19 Acetylation
K19 Ubiquitination
S23 O-Glycosylation
S23 Phosphorylation
S29 Phosphorylation P68400 (CSNK2A1) , P67870 (CSNK2B) , P19784 (CSNK2A2)
Y30 Phosphorylation
S33 Phosphorylation O15111 (CHUK) , P49841 (GSK3B) , P45983 (MAPK8) , Q9H2X6 (HIPK2) , P49840 (GSK3A)
S37 Phosphorylation P49840 (GSK3A) , P45983 (MAPK8) , P49841 (GSK3B) , O15111 (CHUK) , Q9H2X6 (HIPK2)
T41 Phosphorylation P49840 (GSK3A) , P45983 (MAPK8) , O15111 (CHUK) , P49841 (GSK3B)
S45 Phosphorylation O15111 (CHUK) , P48730 (CSNK1D) , P17612 (PRKACA) , P48729 (CSNK1A1) , P49674 (CSNK1E) , Q8N752 (CSNK1A1L) , Q00534 (CDK6) , Q05513 (PRKCZ)
S47 Phosphorylation
K49 Acetylation
K49 Methylation
K49 Ubiquitination
Y64 Phosphorylation Q13882 (PTK6)
S73 Phosphorylation
Y86 Phosphorylation P00519 (ABL1) , P12931 (SRC)
T102 Phosphorylation P68400 (CSNK2A1) , P19784 (CSNK2A2) , P67870 (CSNK2B)
T112 Phosphorylation Q15139 (PRKD1) , P67870 (CSNK2B) , P19784 (CSNK2A2) , P68400 (CSNK2A1)
T120 Phosphorylation Q15139 (PRKD1)
K133 Ubiquitination
Y142 Phosphorylation P04629 (NTRK1) , Q13882 (PTK6) , P21802 (FGFR2) , P22607 (FGFR3) , P06241 (FYN) , P16591 (FER) , P00533 (EGFR)
K158 Ubiquitination
K170 Ubiquitination
S179 Phosphorylation
K180 Ubiquitination
S191 Phosphorylation P45984 (MAPK9) , Q00535 (CDK5)
S196 Phosphorylation
S222 Phosphorylation
K233 Ubiquitination
S246 Phosphorylation Q00535 (CDK5)
K288 Ubiquitination
Y331 Phosphorylation Q13882 (PTK6)
T332 Phosphorylation Q9UQM7 (CAMK2A) , Q13554 (CAMK2B)
Y333 Phosphorylation P12931 (SRC) , Q13882 (PTK6)
K335 Ubiquitination
K345 Acetylation
K345 Ubiquitination
K354 Acetylation
K354 Ubiquitination
T393 Phosphorylation P68400 (CSNK2A1)
K394 Ubiquitination
K435 Acetylation
K435 Ubiquitination
T461 Phosphorylation
T472 Phosphorylation Q13554 (CAMK2B) , Q9UQM7 (CAMK2A)
S473 Phosphorylation
Y489 Phosphorylation P00519 (ABL1)
K496 Ubiquitination
K508 Ubiquitination
T510 Phosphorylation
C520 S-Nitrosylation
T547 Phosphorylation
T551 Phosphorylation
S552 Phosphorylation Q9UQM7 (CAMK2A) , P17612 (PRKACA) , P54646 (PRKAA2) , P31751 (AKT2) , Q13554 (CAMK2B) , P31749 (AKT1)
T556 Phosphorylation
T574 Phosphorylation
S605 Phosphorylation P53778 (MAPK12) , P45984 (MAPK9)
K625 Ubiquitination
S646 Phosphorylation
T653 Phosphorylation
Y654 Phosphorylation P07949 (RET) , P04626 (ERBB2) , P00533 (EGFR) , P00519 (ABL1) , P36888 (FLT3) , P12931 (SRC)
S663 Phosphorylation
Y670 Phosphorylation
K671 Ubiquitination
S675 Phosphorylation O96013 (PAK4) , Q13153 (PAK1) , P17612 (PRKACA)
T679 Phosphorylation
S680 Phosphorylation
S715 Phosphorylation Q05655 (PRKCD)
Y716 Phosphorylation
S718 Phosphorylation P53350 (PLK1)
S721 Phosphorylation
Y724 Phosphorylation
Y748 Phosphorylation

Research Backgrounds

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, 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. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity).

PTMs:

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. 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.

Subcellular Location:

Cytoplasm. Nucleus. Cytoplasm>Cytoskeleton. Cell junction>Adherens junction. Cell junction. Cell membrane. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome. Cytoplasm>Cytoskeleton>Spindle pole. Cell junction>Synapse. Cytoplasm>Cytoskeleton>Cilium basal body.
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. Interaction with FAM53B promotes translocation to the nucleus (PubMed:25183871).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

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).

Subunit Structure:

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. Interacts with CTNND2. Interacts (via the C-terminal region) with CBY1. 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'). Interacts with DLG5 (By similarity). Interacts with FAM53B; promoting translocation to the nucleus. Interacts with TMEM170B. Interacts with AHI1. Interacts with GID8. Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1. Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and HDAC2. Interacts with IRF2BPL; mediates the ubiquitination and degradation of CTNNB1. Interacts with AMFR (By similarity). Interacts with LMBR1L. Interacts with SOX30; prevents interaction of CTNNB1 with TCF7L2/TCF4 and leads to inhibition of Wnt signaling.

(Microbial infection) Interacts with herpes virus 8 protein vPK; this interaction inhibits the Wnt signaling pathway.

Family&Domains:

Belongs to the beta-catenin family.

Research Fields

· 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 > Rap1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Wnt signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Hippo signaling pathway.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Colorectal cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Endometrial cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Thyroid cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Basal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Breast cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Hepatocellular carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Gastric cancer.   (View pathway)

· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).

· Organismal Systems > Immune system > Leukocyte transendothelial migration.   (View pathway)

· Organismal Systems > Endocrine system > Melanogenesis.

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

References

1). Oxysterol-binding protein-like 2 contributes to the developmental progression of preadipocytes by binding to β-catenin. Cell Death Discovery, 2021 (PubMed: 34001864) [IF=7.0]

Application: IHC    Species: zebrafish    Sample: mesencephalon and medulla oblongata

Fig. S4| In zebrafish, Osbpl2b co-localizes with β-catenin.d Tissue sections of the mesencephalon and medulla oblongata in the WT zebrafish were immunostained with anti-β-catenin or anti-Osbpl2b using immunohistochemistry. Arrows pointed the regions of the mesencephalon and medulla oblongata that β-catenin or Osbpl2b localized. Scale bar, 50 μm.

Application: WB    Species: Mice    Sample: WT cells and KO cells

Fig. 2 OSBPL2/ORP2 binds to β-catenin. A Mass spectrometry data of the HEK293T cells expressing FLAG-tagged OSBPL2 were used to identify and evaluated the OSBPL2 interactome and categorized its components by COG and KEGG analyses. B 3T3-L1 preadipocytes were transfected with FLAG-tagged Osbpl2 plasmid for 48 h. Co-IP assays were used to verify the interaction of FLAG-tagged OSBPL2 with endogenous β-catenin in 3T3-L1 preadipocytes. C Panoramic view (right) and amplified view (left) showing the bond between β-catenin (green) and OSBPL2 (rose red). Binding sites 1, ORD in OSBPL2 (Asp-310, Gly-359) and Arm repeats in β-catenin (Ser-351 and Ser-352 residues); binding sites 2, ORD in OSBPL2 (Gln-375, Pro-370, and Thr-368 residues) and Arm repeats in β-catenin (Tyr-604, Pro-606, and Ile-607 residues). D Schematic representing the OSBPL2, β-catenin, and truncated proteins. E Co-IP assays were used to verify the interaction of OSBPL2 with β-catenin or the truncated (N-terminal, SRP, and C-terminal) fractions in HEK293T cells. HEK293T cells co-expressing the truncated HA-tagged (N-terminal) β-catenin and FLAG-tagged OSBPL2 were used as negative controls. F Co-IP assays were used to verify the interaction of β-catenin with the truncated OSBPL2 (ORD). HEK293T cells expressing HA- tagged β-catenin only were used as a negative control. G Co-IP assays were used to verify the interaction of the ORD of OSBPL2 with β-catenin or truncated (SRP or C-terminal) fraction. HEK293T cells expressing HA-tagged β-catenin only were used as a negative control. All data are from three independent experiments. The data are presented as the mean ± SD values (n≥3). ***P < 0.001.

Application: IF/ICC    Species: Mice    Sample: WT cells and KO cells

Fig. 3 Deletion of Osbpl2 reduces the β-catenin level in 3T3-L1 preadipocytes. A, B Lysates of WT and KO cells were immunoblotted for β-catenin, phospho-β-catenin, PPAR-γ, OSBPL2, and ERK1/2 (n=3). The data are normalized to the ERK1/2 control. C WT cells and KO cells at day 0 were fixed and immune-stained with anti-β-catenin (red). Scale bar, 50 μm (inserts, 10 μm). D, E Reduced nuclear localization of β-catenin (imaged by confocal microscope and detected by ZEN software, where a mask is created within the nucleus and the mean pixel intensity of β-catenin within the nucleus is compared to that within the entire cell) related to C. Scale bar, 50 μm (inserts, 10 μm). F WT cells and KO cells were lysed, and the lysates were separated into cytosol and nucleus fractions. The abundance of β-catenin in the two fractions was assessed by western blotting. HISTONE H3 acted as internal nucleus control, and GAPDH acted as internal cytoplasm control (n =3). G β-Catenin were IP with anti-β-catenin antibody in WT preadipocytes or KO preadipocytes and lysates were immunoblotted for ubiquitin detection (n=3). H Lysates of 3T3-L1 preadipocytes transfected with empty vector or FLAG-tagged Osbpl2 plasmid for 48 h were immunoblotted for β-catenin and ERK1/2 detection (n =3). OE=OSBPL2 overexpression. Data are normalized to the ERK1/2 control. All data are from three independent experiments. The data are presented as the mean ± SD values (n≥3). *P < 0.05; **P < 0.01, ***P < 0.001, ns: not significant.

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