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E9902

Sigma-Aldrich

Ephrin-A1/Fc Chimera from mouse

>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Synonym(s):
B61, EFL-1, LERK-1
MDL number:
NACRES:
NA.32

Quality Level

biological source

mouse

recombinant

expressed in NSO cells

assay

>90% (SDS-PAGE)

form

lyophilized powder

potency

0.16-10 ng/mL

mol wt

monomer calculated mol wt 46.8 kDa
50-55 kDa by SDS-PAGE (reducing)

packaging

pkg of 200 μg

storage condition

avoid repeated freeze/thaw cycles

impurities

endotoxin, tested

UniProt accession no.

storage temp.

−20°C

Gene Information

mouse ... Efna1(13636)

Biochem/physiol Actions

EphA1 (ephrin receptor A1) plays an essential role in development, and is involved in the guidance of axonal and cell migration in nervous system. Disruption of ephrin signaling might be involved in the tumorigenesis of clear cell renal cell carcinoma, and absence of EphA1 has a favorable prognosis in the same. It might also be involved in the tumorigenesis and progression of prostate cancer, and might have potential as a marker for prognosis, as well as a therapeutic target. Studies show that it reduces the risk of Alzheimer′s disease, by hindering pathological changes in brain areas such as, hippocampus, lateral occipitotemporal and inferior temporal gyri. In esophageal squamous cells, it acts as differentiation marker. Its expression is elevated in esophageal squamous cell carcinoma, and this relates to advanced stage and metastasis to lymph node.
Member of ephrin ligand family that binds Eph receptor tyrosine kinases (EphA1, EphA2, EphA3, EphA4, EphA5, EphA6, EphA7 and EphB1). Involved in pattern formation and morphogenesis. Ephrin-A1 can be detected on fetal osteoblasts, odotoblasts, chondrocytes, and squamous epithelium. Ephrin-A1 is expressed during embryonic vasculogenesis and during tumor-induced angiogenesis.

Other Notes

Extracellular domain of mouse ephrin-A1 (amino acids 1-182) fused to the C-terminal 6X histidine-tagged Fc region of human IgG.

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 mouse EphA2/Fc in ELISA.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Quotes and Ordering

Augustin DuSablon et al.
PloS one, 12(12), e0189307-e0189307 (2017-12-14)
EphrinA1, a membrane-bound receptor tyrosine kinase ligand expressed in healthy cardiomyocytes, is lost in injured cells following myocardial infarction. Previously, we have reported that a single intramyocardial injection of chimeric ephrinA1-Fc at the time of ischemia reduced injury in the
Hui-Fu Wang et al.
Journal of Alzheimer's disease : JAD, 44(1), 115-123 (2014-09-04)
Ephrin type-A receptor 1 (EPHA1) (11771145) was documented to be one of the most strongly associated locus with Alzheimer's disease (AD) in a recent meta-analysis of five genome wide association studies. However, its contribution to the pathogenesis of AD remains
Libo Peng et al.
International journal of clinical and experimental pathology, 6(9), 1854-1860 (2013-09-17)
The erythropoietin-producing hepatocellular (Eph) family of receptor tyrosine kinases regulates a multitude of physiological and pathological processes. EphA1 is the first member of Eph superfamily and is involved in carcinogenesis. The aim of this study was to investigate the expression
Marieta I Toma et al.
PloS one, 9(7), e102262-e102262 (2014-07-16)
The EPH receptor tyrosine kinases and their cell-bound ligands, the ephrins, have been shown to be associated with cancer development and progression. In this study, mRNA and protein expression of the receptors EPHA1 and EPHA2 as well as of their
Matthieu Chavent et al.
Biochemistry, 53(42), 6641-6652 (2014-10-07)
EphA1 is a receptor tyrosine kinase (RTK) that plays a key role in developmental processes, including guidance of the migration of axons and cells in the nervous system. EphA1, in common with other RTKs, contains an N-terminal extracellular domain, a

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