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Merck

WH0010618M2

Sigma-Aldrich

Monoclonal Anti-TGOLN2 antibody produced in mouse

clone 2F11, purified immunoglobulin, buffered aqueous solution

Synonym(e):

Anti-MGC14722, Anti-TGN38, Anti-TGN46, Anti-TGN48, Anti-TGN51, Anti-TTGN2, Anti-trans-golgi network protein 2

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

2F11, monoclonal

Form

buffered aqueous solution

Speziesreaktivität

human

Methode(n)

immunofluorescence: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

Isotyp

IgG2aκ

GenBank-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... TGOLN2(10618)

Allgemeine Beschreibung

Trans-Golgi network integral membrane protein 2 (TGOLN2) is a heterodimeric type I integral membrane protein. It has a highly conserved N terminus which consists of a signal peptide. The C terminus comprises part of the lumenal domain, a membrane spanning region and cytoplasmic tail.

Immunogen

TGOLN2 (NP_006455, 229 a.a. ~ 327 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
QGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAE

Biochem./physiol. Wirkung

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 to occur. Coupling of the segregation of secretory proteins to the budding of exocytic vesicles is mediated by it. The cytosolic domain of TGOLN2 interacts with AP2 clathrin adaptor complexes and also with the coiled coil region of a protein called neurabin.

Physikalische Form

Solution in phosphate buffered saline, pH 7.4

Rechtliche Hinweise

GenBank is a registered trademark of United States Department of Health and Human Services

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Primate homologues of rat TGN38: primary structure, expression and functional implications.
Ponnambalam S
Journal of Cell Science, 675-685 (1996)
Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin.
Stephens DJ and Banting G
The Journal of Biological Chemistry, 274(42), 30080-30086 (1999)
TGN38/41: a molecule on the move.
Stanley KK and Howell KE
Trends in Cell Biology, 3(8), 252-255 (1993)
K K Stanley et al.
Trends in cell biology, 3(8), 252-255 (1993-08-01)
TGN38/41 is a heterodimeric integral membrane protein that cycles between the trans Golgi network and the cell surface. A tyrosine-containing tetrapeptide motif within its cytoplasmic tail is necessary and sufficient for determining its steady-state location in the TGN. Recent results
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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