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A7107

Sigma-Aldrich

Monoclonal Anti-AP2 antibody produced in mouse

~1.0 mg/mL, clone A6/2/2, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-AP2TF, Anti-TFAP2

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

A6/2/2, monoclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: 2-4 μg/mL using G361 total cell extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TFAP2A(7020)

General description

Adaptor protein-2 (AP2) is a key constituent of clathrin-coated vesicles that mediates the endocytosis of cell membrane components such as G protein-coupled receptors (GPCRs). AP2 is a heterotetramer that consists of α, β, μ and σ subunits which bind to tyrosine- and dileucine-based motifs on membrane-associated cargo proteins.
Monoclonal Anti-AP2 (mouse IgG1 isotype) is derived from the hybridoma A6/2/2 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a peptide corresponding to amino acids of human AP2α. In humans and mice, the adaptor protein-2 (AP2) family comprises five different transcription factors namely AP2α, AP2β, AP2 γ, AP2δ, and AP2ε. These proteins contain N-terminal transactivation domain and C-terminal helix-span-helix motif, which together with a central basic region facilitates dimerization and DNA binding.

Immunogen

peptide corresponding to amino acid 415-433 of human AP2α.

Application

Monoclonal Anti-AP2 antibody produced in mouse has been used in:
  • immunofluorescence staining
  • immunoblotting
  • immunohistochemistry

Biochem/physiol Actions

Adaptor protein-2 (AP2) expression is associated with the embryonic development. AP2β was found to be a tumor specific human telomerase reverse transcriptase (hTERT) promoter activator, suggesting it may be a biomarker for cancer diagnosis or as a cancer therapeutic target for inhibiting hTERT activity and tumor cell growth. In humans, mutations or loss of these genes result in increased tumor growth and metastasis. Specifically, AP2α loss causes down regulation of E-cadherin and matrix metallopeptidase 9 (MMP-9) activity, which in turn enhance tumorigenicity of colon cancer cells. This effect may also be the result of AP2α regulation by p53.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

10 - Combustible liquids

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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Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.
Grenier K, Kontogiannea M, and Fon EA
The Journal of Biological Chemistry, 289(43), 29519-29530 (2014)
AP-2alpha and AP-2gamma are transcriptional targets of p53 in human breast carcinoma cells
Li H, et al.
Oncogene, 25(39), 5405-5405 (2006)
Tumor-specific activation of human telomerase reverses transcriptase promoter activity by activating enhancer-binding protein-2$\beta$ in human lung cancer cells
Deng WG, et al.
The Journal of biological chemistry, 282(36), 26460-26470 (2007)
Loss of AP-2alpha results in deregulation of E-cadherin and MMP-9 and an increase in tumorigenicity of colon cancer cells in vivo.
Schwart B, et al.
Oncogene, 26(28), 4049-4049 (2007)
Roles of telomeres and telomerase in cancer, and advances in telomerase-targeted therapies
Jafri MA, et al.
Genome Medicine, 8(1), 69-69 (2016)

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