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C2206

Sigma-Aldrich

Anti-β-Catenin antibody produced in rabbit

whole antiserum

Synonym(s):

Anti-CTNNB, Anti-EVR7, Anti-MRD19, Anti-NEDSDV, Anti-armadillo

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

mol wt

antigen 88-94 kDa

contains

15 mM sodium azide

species reactivity

several mammalian species

packaging

antibody small pack of 25 μL

technique(s)

dot blot: suitable using the immunogen and related peptides conjugated to BSA
immunocytochemistry: 1:2,000 using cultured MDBK cells
immunohistochemistry: 1:2,000 using bovine kidney frozen sections
western blot: 1:4,000 using cultured MDBK cells

application(s)

research pathology

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CTNNB1(1499)
mouse ... Ctnnb1(12387)
rat ... Ctnnb1(84353)

General description

Catenin are distinct peripheral cytosolic proteins and are classified into α-, β- and γ-catenin (102 kDa, 94 kDa and 86 kDa respectively. It is found in varying abundance in many developing and adult tissues.

Specificity

The antibody does not cross react with α-catenin or γ-catenin (plakoglobin).

Immunogen

synthetic peptide corresponding to the C-terminal region (amino acids 768-781) of human/mouse β-catenin, conjugated with gluteraldehyde to KLH.

Application

Anti-β-Catenin antibody produced in rabbit has been used in
  • co-immunoprecipitation
  • immunoblotting
  • immunofluorescence
  • immunoperoxidase assay

Biochem/physiol Actions

Catenins bind, directly or indirectly, to the conserved cytoplasmic tail domain of the cell adhesion cadherins. The protein, β-catenin, binds directly to the cytoplasmic tail of E-cadherin. Plakoglobin (probably identical to γ-catenin) and β-catenin are structural and possibly functional mammalian homologues of armadillo (arm), a Drosophila protein involved in signal transduction. It binds to the amino terminus of α-catenin and also interacts with the cytosolic protein product of the human tumor suppressor gene Adenomatous polyposis coli (APC). The central core region of β-catenin is involved in mediation of the interaction of cadherin-catenin complex with the epidermal growth factor receptor. The protein, β-catenin, is the target of two signal transduction pathways mediated by the protooncogenes Src and wingless-related integration site (Wnt-1). p120cas which exhibits structural similarity to β-catenin and plakoglobin may represent another catenin associated with cadherin.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Dysregulation of ubiquitin homeostasis and beta-catenin signaling promote spinal muscular atrophy
Wishart TM, et al.
The Journal of Clinical Investigation, 124(4), 1821-1834 (2014)
Defining E-cadherin-associated protein complexes in epithelial cells: plakoglobin, beta-and gamma-catenin are distinct components
Piepenhagen PA and Nelson WJ
Journal of Cell Science, 104(3), 751-762 (1993)
Antipsychotics alter the protein expression levels of beta-catenin and GSK-3 in the rat medial prefrontal cortex and striatum
Alimohamad H, et al.
Biological Psychiatry, 57(5), 533-542 (2005)
Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene
Aoki K and Taketo MM
Journal of Cell Science, 120(19), 3327-3335 (2007)
Roman Schoenauer et al.
Basic research in cardiology, 106(2), 233-247 (2010-11-12)
The M-band is the prominent cytoskeletal structure that cross-links the myosin and titin filaments in the middle of the sarcomere. To investigate M-band alterations in heart disease, we analyzed the expression of its main components, proteins of the myomesin family

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