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Recombinant Mouse EphA3 Fc Chimera Protein, CF

Catalog #: 640-A3
6 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
640-A3-200
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Citations (6)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse EphA3 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized rmEphA3/Fc Chimera at 2 µg/mL (100 µL/well) can bind rhEphrin A5 Fc Chimera with a linear range of 0.08-5 ng/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived mouse EphA3 protein
Mouse EphA3
Glu21 - His541 (Thr323Ala & Glu476Gln)
Accession # Q8BRB1		 IEGRMD Human IgG1
(Pro100 - Lys330)		 6-His tag
N-terminus C-terminus
Accession #
Q8BRB1
N-terminal Sequence
Analysis
Glu21
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
86 kDa (monomer)
SDS-PAGE
110 kDa, reducing conditions

Product Datasheets

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640-A3

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

640-A3

Formulation Lyophilized from a 0.2 μm filtered solution in Tris.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: EphA3

EphA3, also known as Cek4, Mek4, Hek, Tyro4, and Hek4, is a 135 kDa glycosylated member of the transmembrane Eph receptor tyrosine kinase family. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA3 preferentially binds to Ephrin-A5. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). The 520 amino acid (aa) extracellular domain (ECD) of mouse EphA3 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type II domains. The 419 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (3, 4). Within the ECD, mouse EphA3 shares 96% and 98% aa sequence identity with human and rat EphA3, respectively. Alternate splicing generates a secreted isoform that consists of nearly the entire ECD. EphA3 is expressed in the developing forebrain, retinal axons, some spinal cord motor neurons, and the heart where it plays an important role in axonal repulsion and organ morphogenesis (5 ‑ 8). It is upregulated on some hematopoietic and solid tumor cells and on astrocytes surrounding injured nervous tissue (5, 9 - 11). EphA3 ligation inhibits cellular adhesion to fibronectin as well as cellular migration (9, 10). Transmembrane EphA3 associates in cis with ADAM10 which then promotes the cleavage in trans of Ephrin-A5 (12). It also associates in cis with Ephrin-A5 on retinal axons, thereby preventing the activation of EphA3 by Ephrin-A (13). Multiple tyrosine residues within the cytoplasmic region of EphA3 become phosphorylated during ligand-induced signaling (14, 15).

References
  1. Pasquale, E.B. (2005) Nat. Rev. Mol. Cell Biol. 6:462.
  2. Merlos-Suarez, A. and E. Batlle (2008) Curr. Opin. Cell Biol. 20:194.
  3. Sajjadi, F.G. et al. (1991) New Biol. 3:769.
  4. Lackmann, M. et al. (1998) J. Biol. Chem. 273:20228.
  5. Chiari, R. et al. (2000) Cancer Res. 60:4855.
  6. Kudo, C. et al. (2005) J. Comp. Neurol. 487:255.
  7. Kilpatrick, T.J. et al. (1996) Mol. Cell. Neurosci. 7:62.
  8. Stephen, L.J. et al. (2007) Dev. Biol. 302:66.
  9. Smith, L.M. et al. (2004) Exp. Cell Res. 292:295.
  10. Clifford, N. et al. (2008) J. Cell. Biochem. 105:1250.
  11. Irizarry-Ramirez, M. et al. (2005) J. Neurotrauma 22:929.
  12. Janes, P.W. et al. (2005) Cell 123:291.
  13. Carvalho, R.F. et al. (2006) Nat. Neurosci. 9:322.
  14. Shi, G. et al. (2010) Cell Res. June epub.
  15. Hu, T. et al. (2009) Biochemistry 48:6369.
Long Name
Eph Receptor A3
Entrez Gene IDs
2042 (Human); 13837 (Mouse)
Alternate Names
Cek4; EC 2.7.10; EC 2.7.10.1; EK4; EPH receptor A3; EphA3; EPH-like kinase 4; ephrin type-A receptor 3; ETK; Hek4; HEKETK1eph-like tyrosine kinase 1; human embryo kinase 1; TYRO4 protein tyrosine kinase; Tyro4; Tyrosine-protein kinase receptor ETK1; Tyrosine-protein kinase TYRO4

Citations for Recombinant Mouse EphA3 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

6 Citations: Showing 1 - 6
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  1. IL-26 mediates epidermal growth factor receptor-tyrosine kinase inhibitor resistance through endoplasmic reticulum stress signaling pathway in triple-negative breast cancer cells
    Authors: T Itoh, R Hatano, Y Horimoto, T Yamada, D Song, H Otsuka, Y Shirakawa, S Mastuoka, N Iwao, TM Aune, NH Dang, Y Kaneko, K Okumura, C Morimoto, K Ohnuma
    Cell Death & Disease, 2021-05-21;12(6):520.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Thalamic afferents influence cortical progenitors via ephrin A5-EphA4 interactions
    Authors: K Gerstmann, D Pensold, J Symmank, M Khundadze, CA Hübner, J Bolz, G Zimmer
    Development, 2014-12-05;142(1):140-50.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Development of the prethalamus is crucial for thalamocortical projection formation and is regulated by Olig2.
    Authors: Ono, Katsuhik, Clavairoly, Adrien, Nomura, Tadashi, Gotoh, Hitoshi, Uno, Aoi, Armant, Olivier, Takebayashi, Hirohide, Zhang, Qi, Shimamura, Kenji, Itohara, Shigeyos, Parras, Carlos M, Ikenaka, Kazuhiro
    Development, 2014-05-01;141(10):2075-84.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Temporal regulation of ephrin/Eph signalling is required for the spatial patterning of the mammalian striatum.
    Authors: Passante L, Gaspard N, Degraeve M, Frisen J, Kullander K, De Maertelaer V, Vanderhaeghen P
    Development, 2008-08-28;135(19):3281-90.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Bioassay
  5. Ephrin A/EphA controls the rostral turning polarity of a lateral commissural tract in chick hindbrain.
    Authors: Zhu Y, Guthrie S, Murakami F
    Development, 2006-10-01;133(19):3837-46.
    Species: Chicken
    Sample Types: Whole Tissue
    Applications: Bioassay
  6. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.
    Authors: Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, Blobel CP, Himanen JP, Lackmann M, Nikolov DB
    Cell, 2005-10-21;123(2):291-304.
    Species: Human
    Sample Types: Whole Cells
    Applications: Immunoprecipitation

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