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C2081

Sigma-Aldrich

Anti-α-Catenin antibody produced in rabbit

whole antiserum

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Synonym(s):
Anti-α-Catenin, Alpha Catenin Antibody, Alpha Catenin Antibody - Anti-α-Catenin antibody produced in rabbit
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 ~102 kDa

contains

15 mM sodium azide

species reactivity

several mammalian species

technique(s)

dot blot: suitable using α-catenin peptide amino acids 890-901 conjugated to BSA
immunohistochemistry (frozen sections): 1:2,000 using bovine kidney sections
indirect immunofluorescence: 1:2,000 using cultured MDBK cells
microarray: suitable
western blot: 1:4,000 using cultured MDBK cells extract

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CTNNA1(1495)
mouse ... Ctnna1(12385)
rat ... Ctnna1(307505)

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General description

Catenin are distinct peripheral cytosolic proteins, α, β, and γ -catenin (102 kDa, 94 kDa and 86 kDa, respectively) are found in varying abundance in many developing and adult tissues. Within its conserved regions, α-catenin shows 30% identity to vinculin, a protein found mainly in focal cell-cell and cell substrate adhesions.

Specificity

Does not cross-react with β-catenin or γ-catenin (plakoglobin).

Immunogen

synthetic peptide corresponding to the C-terminal region (amino acids 890-901) of human/mouse α-catenin conjugated to KLH.

Application

Anti-α-Catenin antibody has been used:
  • in dot blot immunoassay
  • in immunoblotting
  • in immunofluorescence
  • in western blotting
  • in immunoprecipitation
  • in immunofluorescence staining
  • in coimmunoprecipitation

Biochem/physiol Actions

Catenins bind, directly or indirectly, to the conserved cytoplasmic tail domain of the cell-adhesion cadherins. Cadherins are transmembrane cell surface glycoprotein molecules that mediate calcium-dependent intercellular interactions and are important for tissue morphogenesis. Catenins link E-cadherin to other integral membrane proteins such as Na+ /K+ -ATPase, or to cytoplasmic proteins such as fodrin, ankyrin, sarcoma (Src) and Yes kinases and are modulated by Wnt-1 protooncogene. They are considered good candidates for mediating transduction of cell-cell contact positional signals to the cell interior. α-Catenin appears to be capable of interacting with N-cadherin and P-cadherin. Absence of α-catenin is found in certain tumor cell lines. Frequent reduction of α-catenin levels in human carcinomas of the esophagus, stomach and colon is also reported. Prostate cancer development appears to be correlated with α-catenin gene deletions.

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.

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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alpha-catenin: at the junction of intercellular adhesion and actin dynamics
Kobielak A and Fuchs E
Nature Reviews in Molecular and Cell Biology, 5(8), 614-614 (2004)
Structure and biochemistry of cadherins and catenins
Shapiro L and Weis W I
Cold Spring Harbor Perspectives in Biology, 1(3), a003053-a003053 (2009)
Cardiac tissue-restricted deletion of plakoglobin results in progressive cardiomyopathy and activation of beta-catenin signaling
Li J, et al.
Molecular and cellular biology, 31(6), 1134-1144 (2011)
Huapeng H Yu et al.
Journal of cell science, 129(1), 80-94 (2015-11-21)
In vertebrate epithelia, p120-catenin (hereafter referred to as p120; also known as CTNND1) mediates E-cadherin stability and suppression of RhoA. Genetic ablation of p120 in various epithelial tissues typically causes striking alterations in tissue function and morphology. Although these effects
Cadherins and catenins in development
Huber O, et al.
Current Opinion in Cell Biology, 8(5), 685-691 (1996)

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