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E4156

Sigma-Aldrich

Anti-Early Endosomal Antigen 1 (N-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-EEA1, Anti-Endosome-associated Protein p162, Anti-Zinc Finger FYVE Domain-containing Protein 2

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About This Item

MDL number:
MFCD01633310
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~160 kDa

species reactivity

mouse, human, rat

concentration

~1 mg/mL

technique(s)

indirect immunofluorescence: 5-10 μg/mL using human HeLa and rat NRK cells
western blot (chemiluminescent): 0.4-0.8 μg/mL using whole extract of mouse NIH-3T3 cells

UniProt accession no.

Q15075

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... EEA1(8411)
mouse ... Eea1(216238)
rat ... Eea1(314764)

Related Categories

General description

The gene Early Endosome Antigen 1 (EEA1) encodes for around 1400 amino acid proteins. It is a peripheral membrane protein associated with the cytoplasmic face of early endosomes. It is a 162 kDa autoantigen protein. EEA1 is a dimer, which comprises extensive coiled-coil regions. At its C-terminus, it contains a cysteine-rich zinc-finger-like domain named FYVE domain. This FYVE domain is conserved from yeast to man. FYVE domain is implicated in the specific localization of EEA1 to endosomes.

Immunogen

synthetic peptide corresponding amino acid residues 24-40 of human EEA1 with C-terminal added cysteine, conjugated to KLH. The corresponding sequence is identical in mouse.

Application

Anti-Early Endosomal Antigen 1 (N-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

Early Endosomal Antigen 1 (EEA1) localization in endosomes is implicated in subacute systemic lupus erythematosus. Endosomal targeting of EEA1 also requires its binding to the active form of the small GTPase Rab5. The binding of EEA1 to phosphatidylinositol 3 phosphate (PtdInsP) and rabaptin-5 (Rab5)-GTP is essential for the localization and function of EEA1 in endocytic membrane fusion. Anti-EEA1 may be used as an early endosome marker.

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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Andree Hubber et al.
Scientific reports, 7, 44795-44795 (2017-03-21)
The evolutionarily conserved processes of endosome-lysosome maturation and macroautophagy are established mechanisms that limit survival of intracellular bacteria. Similarly, another emerging mechanism is LC3-associated phagocytosis (LAP). Here we report that an intracellular vacuolar pathogen, Legionella dumoffii, is specifically targeted by
EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts
Wilson JM, et al.
Molecular Biology of the Cell, 11(8), 2657-2671 (2000)
Jan Schulze-Luehrmann et al.
Cellular microbiology, 18(2), 181-194 (2015-08-08)
The obligate intracellular pathogen Coxiella burnetii replicates in a large phagolysosomal-like vacuole. Currently, both host and bacterial factors required for creating this replicative parasitophorous C. burnetii-containing vacuole (PV) are poorly defined. Here, we assessed the contributions of the most abundant
FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
Raiborg C, et al.
Journal of Cell Science, 114(12), 2255-2263 (2001)
Ziying Fu et al.
Frontiers in cellular neuroscience, 12, 71-71 (2018-04-05)
The main olfactory epithelium (MOE) functions to detect odor molecules, provide an epithelial surface barrier, and remove xenobiotics from inhaled air. Mechanisms coordinating the activities of different cell types within the MOE to maintain these functions are poorly understood. Previously
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