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Key Documents

SAB4200355

Sigma-Aldrich

Anti-TGN46 antibody, Mouse monoclonal

clone TGN46-8, purified from hybridoma cell culture

Synonyme(s) :

Anti-Trans-Golgi network protein, 46-kD

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

TGN46-8, monoclonal

Forme

buffered aqueous solution

Poids mol.

80-100 kDa

Espèces réactives

human

Concentration

~1.0 mg/mL

Technique(s)

indirect immunofluorescence: 5-10 μg/mL using HeLa cells
western blot: 2-4 μg/mL using whole extracts of HEK-293T cells over-expressing human TGN46

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 ... TGOLN2(10618)

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Description générale

Trans-Golgi network integral membrane protein 2 (TGOLN2), also known as trans-Golgi network 46 (TGN46), is encoded by the gene mapped to human chromosome 2p11.2. It is a heterodimeric type I integral membrane protein. TGOLN2 has a highly conserved N terminus, which consists of a signal peptide. The C terminus possesses a lumenal domain, a membrane spanning region and cytoplasmic tail.

Immunogène

synthetic peptide corresponding to the C-terminal region of human TGN46, conjugated to KLH. The corresponding sequence is identical in monkey and differs by 3 amino acids in rat and mouse TGN46.

Actions biochimiques/physiologiques

Trans-Golgi network integral membrane protein 2 (TGOLN2) cycles between the trans-Golgi network (TGN) and the cell surface via an early endosomal compartment. This movement is mediated by a tyrosine-based tetra peptide signal (SDYQRL) in the cytoplasmic domain. It plays an important role in the formation of exocytic vesicles at the TGN by functioning as a receptor for complexes of a cytoplasmic protein known as p62 and one GTP-binding protein. The cytoplasmic domain of TGOLN2 binds to the complex and is essential for budding process. It mediates the coupling of the segregation of secretory proteins to the budding of exocytic vesicles. The cytosolic domain of TGOLN2 interacts with AP2 clathrin adaptor complexes and also with the coiled coil region of a protein called neurabin.

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

12 - Non 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

Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin.
The Journal of Biological Chemistry (1999)
TGN38/41: a molecule on the move.
Trends in Cell Biology (1993)
Primate homologues of rat TGN38: primary structure, expression and functional implications.
Journal of Cell Science (1996)
Molecular cloning and expression of a novel human trans-Golgi network glycoprotein, TGN51, that contains multiple tyrosine-containing motifs.
Kain R
The Journal of Biological Chemistry (1998)
Mahdi Mojallal et al.
Nature communications, 5, 4557-4557 (2014-08-02)
The establishment and maintenance of apical-basal cell polarity is essential for the functionality of glandular epithelia. Cell polarity is often lost in advanced tumours correlating with acquisition of invasive and malignant properties. Despite extensive knowledge regarding the formation and maintenance

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