Recombinant Mouse EphA2 Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Mouse EphA2 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to bind Recombinant Mouse Ephrin‑A1 Fc Chimera (Catalog # 602-A1) in a functional ELISA.
  Immobilized Recombinant Mouse EphA2 Fc Chimera at 2 µg/mL (100 µL/well) can bind Recombinant Mouse Ephrin-A1 Fc Chimera with a linear range of 0.078-5 ng/mL.
  Optimal dilutions should be determined by each laboratory for each application.
• Source: Mouse myeloma cell line, NS0-derived mouse EphA2 protein
  

  Mouse EphA2 (Ala22-Ala535) Accession # AAA82113	IEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: AAA82113
• N-terminal Sequence: Ala22
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Epha2
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 84 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 105 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in Tris-HCl and EDTA.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse EphA2 Fc Chimera Protein, CF

• ARCC2
• EC 2.7.10
• EC 2.7.10.1
• Eck
• ECKepithelial cell receptor protein tyrosine kinase
• EPH receptor A2
• EphA2
• ephrin type-A receptor 2
• Epithelial cell kinase
• Myk2
• Sek2
• soluble EPHA2 variant 1
• Tyrosine-protein kinase receptor ECK

Background

EphA2, also known as Eck, Myk2, and Sek2 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphA2 has been shown to bind ephrin-A3, ephrin-A1, ephrin-A5, ephrin-A4, and ephrin-A2 (2, 3). The extracellular domains of mouse and human EphA2 share greater than 92% amino acid identity. Only membrane-bound or Fc‑clustered ligands are capable of activating the receptor in vitro. While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin families also appear to play a role in angiogenesis (3).

1. Eph Nomenclature Committee [letter] (1997) Cell 90:403.
2. Flanagan, J.G. and P. Vanderhaegen (1998) Annu. Rev. Neurosci. 21:309.
3. Pasquale, E.B. (1997) Curr. Opin. Cell. Biol. 9:608.

Publications for EphA2 (639-A2)(11)

Publications using 639-A2

• El Fakiri, M;Regupathy, AR;Uhlmann, L;Ayada, N;Geis, NM;Domogalla, LC;Lahdenranta, J;Blakeman, B;Wood, F;Meyer, PT;Huxley, P;Eder, M;Mudd, GE;Eder, AC; Development and preclinical characterization of a novel radiotheranostic EphA2-targeting bicyclic peptide Theranostics 2024-08-06 [PMID: 39239524] (Bioassay, Mouse)
• S Kohara, K Ogawa Eph/Ephrin Promotes the Adhesion of Liver Tissue-Resident Macrophages to a Mimicked Surface of Liver Sinusoidal Endothelial Cells Biomedicines, 2022-12-12;10(12):. 2022-12-12 [PMID: 36551990] (Bioassay, Mouse)
• TK Darling, PN Mimche, C Bray, B Umaru, LM Brady, C Stone, CE Eboumbou M, TE Lane, LS Ayong, TJ Lamb EphA2 contributes to disruption of the blood-brain barrier in cerebral malaria PLoS Pathog., 2020-01-30;16(1):e1008261. 2020-01-30 [PMID: 31999807] (Bioassay, In Vivo, Mouse)
• M Takasugi, R Okada, A Takahashi, D Virya Chen, S Watanabe, E Hara Small extracellular vesicles secreted from senescent cells promote cancer cell proliferation through EphA2 Nat Commun, 2017-06-06;8(0):15729. 2017-06-06 [PMID: 28585531] (Bioassay, Mouse)
• Ullman C, Mathonet P, Oleksy A, Diamandakis A, Tomei L, Demartis A, Nardi C, Sambucini S, Missineo A, Alt K, Hagemeyer C, Harris M, Hedt A, Weis R, Gehlsen K High Affinity Binders to EphA2 Isolated from Abdurin Scaffold Libraries; Characterization, Binding and Tumor Targeting. PLoS ONE, 2015-08-27;10(8):e0135278. 2015-08-27 [PMID: 26313909] (Bioassay, Human)
• Ieguchi K, Tomita T, Omori T, Komatsu A, Deguchi A, Masuda J, Duffy S, Coulthard M, Boyd A, Maru Y ADAM12-cleaved ephrin-A1 contributes to lung metastasis. Oncogene, 2013-05-20;33(17):2179-90. 2013-05-20 [PMID: 23686306] (In Vivo, Mouse)
• Giorgio C, Hassan Mohamed I, Flammini L, Barocelli E, Incerti M, Lodola A, Tognolini M Lithocholic acid is an Eph-ephrin ligand interfering with Eph-kinase activation. PLoS ONE, 2011-03-30;6(3):e18128. 2011-03-30 [PMID: 21479221] (Binding Assay, Human)
• Afshari FT, Kwok JC, Fawcett JW Astrocyte-produced ephrins inhibit schwann cell migration via VAV2 signaling. J. Neurosci., 2010-03-24;30(12):4246-55. 2010-03-24 [PMID: 20335460] (Bioassay, Rat)
• Cercone MA, Schroeder W, Schomberg S, Carpenter TC EphA2 receptor mediates increased vascular permeability in lung injury due to viral infection and hypoxia. Am. J. Physiol. Lung Cell Mol. Physiol., 2009-08-14;297(5):L856-63. 2009-08-14 [PMID: 19684201] (In Vivo, Rat)
• Jackson D, Gooya J, Mao S, Kinneer K, Xu L, Camara M, Fazenbaker C, Fleming R, Swamynathan S, Meyer D, Senter PD, Gao C, Wu H, Kinch M, Coats S, Kiener PA, Tice DA A human antibody-drug conjugate targeting EphA2 inhibits tumor growth in vivo. Cancer Res., 2008-11-15;68(22):9367-74. 2008-11-15 [PMID: 19010911] (Binding Assay)
• Dobrzanski P, Hunter K, Jones-Bolin S, Chang H, Robinson C, Pritchard S, Zhao H, Ruggeri B Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist. Cancer Res., 2004-02-01;64(3):910-9. 2004-02-01 [PMID: 14871820] (Bioassay, In Vivo, Mouse, Rat)

Bioinformatics

• Gene Symbol: Epha2
• Uniprot:
  • AAA82113()