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E8034

Monoclonal Anti-EEA1 antibody produced in mouse

~1.0 mg/mL, clone EEA1-C33, purified immunoglobulin, buffered aqueous solution

Synonym(e):

Anti-Early endosomal antigen 1, Anti-MST105, Anti-MSTP105, Anti-ZFYVE2

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Über diesen Artikel

UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
EEA1-C33, monoclonal
Application:
WB
Citations:
10

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

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
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
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
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
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

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