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SAB4200355

Sigma-Aldrich

Anti-TGN46 antibody, Mouse monoclonal

clone TGN46-8, purified from hybridoma cell culture

Synonym(s):

Anti-Trans-Golgi network protein, 46-kD

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About This Item

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

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

TGN46-8, monoclonal

form

buffered aqueous solution

mol wt

80-100 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TGOLN2(10618)

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General description

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.

Immunogen

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.

Biochem/physiol Actions

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.

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

12 - Non 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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Primate homologues of rat TGN38: primary structure, expression and functional implications.
Journal of Cell Science (1996)
TGN38/41: a molecule on the move.
Trends in Cell Biology (1993)
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)
Kamal L Nahas et al.
PLoS pathogens, 18(7), e1010629-e1010629 (2022-07-08)
Herpes simplex virus-1 (HSV-1) is a large, enveloped DNA virus and its assembly in the cell is a complex multi-step process during which viral particles interact with numerous cellular compartments such as the nucleus and organelles of the secretory pathway.
Ryoko Ando et al.
Nature methods (2023-12-01)
Although StayGold is a bright and highly photostable fluorescent protein, its propensity for obligate dimer formation may hinder applications in molecular fusion and membrane targeting. To attain monovalent as well as bright and photostable labeling, we engineered tandem dimers of

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