E8152
EphA3/Fc Chimera from mouse
>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
Synonym(s):
Cek4, Hek, Hek4, Mek4, Tyro4
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About This Item
UNSPSC Code:
51111800
MDL number:
biological source
mouse
recombinant
expressed in NSO cells
assay
>90% (SDS-PAGE)
form
lyophilized powder
mol wt
monomer calculated mol wt 86 kDa, ~110 kDa by SDS-PAGE (reducing)
storage condition
avoid repeated freeze/thaw cycles (Do not store in a frost-free freezer.)
technique(s)
ligand binding assay: suitable
impurities
endotoxin, tested
UniProt accession no.
storage temp.
−20°C
Gene Information
mouse ... Epha3(13837)
General description
EPHA3 is a receptor tyrosine kinase (RTK) belonging to the largest subgroup of RTKs called ephrin group of receptors. It has a high level of expression from placental stage through the whole developmental process. It is a type I transmembrane protein, and has a membrane-bound ligand. It is both an oncogene and a tumor-suppressor gene. This protein resides in both the cytosol and the plasma membrane.
Biochem/physiol Actions
EPHA3 binds the ephrin-A ligand and has diverse cellular function. Analysis of human colorectal, breast, lung and pancreatic cancer samples shows somatic mutations in the EPHA3 gene. EPHA3 gene expression can be regulated by CD28 and IGF-1 in Jurkat cells and expression of EPHA3 is associated with adherence and motility of malignant T cells. It maintains the less differentiated state of cancer cells, by activating MAPK (mitogen-activated protein kinase) pathway. It is over-expressed in glioblastoma (GBM) cells, especially during the initial stages. It also higher expression levels in aggressive mesenchymal subtype of GBM. In hepatocellular carcinoma (HCC), it predicts increased invasiveness and poor patient prognosis.
Member of the Eph receptor tyrosine kinase family shown to bind ephrin-A1, ephrin-A2, ephrin-A3, ephrin-A4, ephrin-A5, and ephrin-B1; involved in pattern formation and morphogenesis.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.
Analysis Note
The biological activity is measured by its ability to bind recombinant human ephrin-A5/Fc in an ELISA.
Other Notes
Extracellular domain of mouse EphA3 (amino acids 1-541) fused by means of a polypeptide linker to the Fc region of human IgG1 that is histidine tagged at the C-terminus.
flash_point_f
Not applicable
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Cheng-Yi Lu et al.
Oncology reports, 30(5), 2179-2186 (2013-08-24)
Although EphA3 expression has been associated with progression or prognosis in several types of tumors, the role of EphA3 in hepatocellular carcinoma (HCC) remains unknown. This study sought to investigate the clinicopathological and prognostic relevance of EphA3 expression in HCC
Loraine M Smith et al.
Experimental cell research, 292(2), 295-303 (2003-12-31)
Stimulation of CD28 alone has been shown to regulate cytokine gene transcription and expression of the type 1 insulin-like growth factor receptor (IGF-1R) in lymphocytes. In this study, the ephrin receptor tyrosine kinase ephA3, was identified as a new CD28-responsive
Laura D Wood et al.
Human mutation, 27(10), 1060-1061 (2006-08-31)
Tyrosine kinases are major regulators of signal transduction cascades involved in cellular proliferation and have important roles in tumorigenesis. We have recently analyzed the tyrosine kinase gene family for alterations in human colorectal cancers and identified somatic mutations in seven
Structural recognition of an optimized substrate for the ephrin family of receptor tyrosine kinases.
Tara L Davis et al.
The FEBS journal, 276(16), 4395-4404 (2009-08-15)
Ephrin receptor tyrosine kinase A3 (EphA3, EC 2.7.10.1) is a member of a unique branch of the kinome in which downstream signaling occurs in both ligand- and receptor-expressing cells. Consequently, the ephrins and ephrin receptor tyrosine kinases often mediate processes
Jenni Lahtela et al.
Cell cycle (Georgetown, Tex.), 12(4), 625-634 (2013-01-18)
Activation of a cellular senescence program is a common response to prolonged oncogene activation or tumor suppressor loss, providing a physiological mechanism for tumor suppression in premalignant cells. The link between senescence and tumor suppression supports the hypothesis that a
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