E4156
Anti-Early Endosomal Antigen 1 (N-terminal) antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
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Synonym(s):
Anti-EEA1, Anti-Endosome-associated Protein p162, Anti-Zinc Finger FYVE Domain-containing Protein 2
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biological source
rabbit
Quality Level
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.
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.
related product
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Find documentation for the products that you have recently purchased in the Document Library.
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)
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
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)
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
Distinct lysosomal network protein profiles in Parkinsonian syndrome cerebrospinal fluid
Boman A, et al.
Journal of Parkinson's Disease, 6(2), 307-315 (2016)
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