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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

Synonyme(s) :

Anti-AP2TF, Anti-TFAP2

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

A6/2/2, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~50 kDa

Espèces réactives

human

Concentration

~1.0 mg/mL

Technique(s)

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

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... TFAP2A(7020)

Description générale

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.

Immunogène

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
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)
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)
Li E Yang et al.
Journal of the American Society of Nephrology : JASN, 16(10), 2890-2896 (2005-08-19)
During acute hypertension, Na(+)/H(+) exchangers (NHE3) retract from top to base of proximal tubule microvilli (MV) and Na(+) reabsorption decreases in proximal tubule. This study aimed to determine whether the actin-based motor myosin VI coordinately retracts with NHE3 in response

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