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Merck

E4156

Sigma-Aldrich

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

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

Sinónimos:

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

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen ~160 kDa

reactividad de especies

mouse, human, rat

concentración

~1 mg/mL

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

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

Descripción general

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.

Inmunógeno

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.

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Forma física

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

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


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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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