E8034
Monoclonal Anti-EEA1 antibody produced in mouse
~1.0 mg/mL, clone EEA1-C33, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-Early endosomal antigen 1, Anti-MST105, Anti-MSTP105, Anti-ZFYVE2
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About This Item
UNSPSC Code:
12352203
conjugate:
unconjugated
application:
WB
clone:
EEA1-C33, monoclonal
species reactivity:
human, mouse, rat
citations:
10
technique(s):
western blot: 2-4 μg/mL using whole extract of rat NRK or human HeLa cells
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
EEA1-C33, monoclonal
form
buffered aqueous solution
mol wt
antigen ~160 kDa
species reactivity
human, mouse, rat
concentration
~1.0 mg/mL
technique(s)
western blot: 2-4 μg/mL using whole extract of rat NRK or human HeLa cells
isotype
IgG1
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)
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. EEA1 is a autoantigen associated with subacute cutaneous systemic lupus erythematosus and is a coiled-coil protein localized to early endosomes and cytosol.
Application
Monoclonal Anti-EEA1 antibody produced in mouse is suitable for the following applications:
- Western blotting (at a concentration of 2-4μg/mL using whole extract of rat NRK or human HeLa cells)
- Immunofluorescence Analysis
- Immunocytochemistry
Biochem/physiol Actions
Early Endosome Antigen 1 (EEA1) controls vesicle fusion during endocytosis. In neurons, it is involved in recycling of synaptic vesicles and neurotransmitter receptors. Patients with neurological deficits develop EEA1 autoantibodies. Mutation in EEA1 gene leads to susceptibility to diabetes in the Japanese population. Phosphatidylinositol 3-phosphate (PtdIns(3)P) is essential for the localization and function of EEA1.
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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Chae-ryun Yi et al.
Journal of virology, 82(11), 5307-5315 (2008-03-28)
Abelson murine leukemia virus (Ab-MLV) arose from a recombination between gag sequences in Moloney MLV (Mo-MLV) and the c-abl proto-oncogene. The v-Abl oncoprotein encoded by Ab-MLV contains MA, p12, and a portion of CA sequences derived from the gag gene
Mafalda Lopes da Silva et al.
Traffic (Copenhagen, Denmark), 13(10), 1351-1363 (2012-07-12)
The obligate intracellular liver stage of the Plasmodium parasite represents a bottleneck in the parasite life cycle and remains a promising target for therapeutic intervention. During this stage, parasites undergo dramatic morphological changes and achieve one of the fastest replication
Teddy Grand et al.
Kidney international, 76(9), 999-1005 (2009-08-07)
Dent's disease is an X-linked recessive disorder affecting the proximal tubules and is frequently associated with mutations in CLCN5, which encodes the electrogenic chloride-proton exchanger ClC-5. To better understand the functional consequences of CLCN5 mutations in this disease, we screened
Annalisa Carlucci et al.
The Journal of biological chemistry, 285(50), 39260-39270 (2010-10-07)
PTPD1, a cytosolic non-receptor protein-tyrosine phosphatase, stimulates the Src-EGF transduction pathway. Localization of PTPD1 at actin cytoskeleton and adhesion sites is required for cell scattering and migration. Here, we show that during EGF stimulation, PTPD1 is rapidly recruited to endocytic
Christoph Kaether et al.
Traffic (Copenhagen, Denmark), 7(4), 408-415 (2006-03-16)
Alzheimer's disease is characterized by brain deposition of extracellular amyloid beta-peptide (Abeta)-containing plaques. The cellular site of gamma-secretase activity, which releases Abeta and the corresponding amyloid precursor protein intracellular domain (AICD), remains controversial. Proposed cleavage sites range from the endoplasmic
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