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Recombinant Human Ephrin-A4 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human Ephrin-A4 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmEphA7/Fc Chimera at 2 µg/mL (100 µL/well) can bind rhEphrin-A4/Fc Chimera with a linear range of 0.16-10 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-A4 protein
Human Ephrin-A4
(Leu26 - Gly171)
Accession # P52798
IEGRMD Human IgG1
(Pro100 - Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu26
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
EFNA4
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
43.7 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
50 kDa, reducing conditions
Publications
Read Publications using
369-EA in the following applications:

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 PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
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 Human Ephrin-A4 Fc Chimera Protein, CF

  • EFL4
  • EFL-4
  • EFNA4
  • EPH-related receptor tyrosine kinase ligand 4
  • EphrinA4
  • Ephrin-A4
  • EPLG4MGC125826
  • LERK-4
  • LERK4FLJ57652
  • ligand of eph-related kinase 4

Background

Ephrin-A4, also known as LERK-4 and EFL-4, (1) is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The A-class ligands have a GPI anchor following the conserved sequence. Ephrin-A4 has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1 (2, 3). The extracellular domains of human and mouse Ephrin-A4 share 80% 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.

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Publications for Ephrin-A4 (369-EA)(6)

We have publications tested in 3 confirmed species: Human, Mouse, Virus - Henipavirus.

We have publications tested in 3 applications: Bioassay, Control, Coprecipitation Assay.


Filter By Application
Bioassay
(3)
Control
(1)
Coprecipitation Assay
(1)
All Applications
Filter By Species
Human
(4)
Mouse
(1)
Virus - Henipavirus
(1)
All Species
Showing Publications 1 - 6 of 6.
Publications using 369-EA Applications Species
YL Chen, YC Yen, CW Jang, SH Wang, HT Huang, CH Chen, JR Hsiao, JY Chang, YW Chen Ephrin A4-ephrin receptor A10 signaling promotes cell migration and spheroid formation by upregulating NANOG expression in oral squamous cell carcinoma cells Scientific Reports, 2021-01-12;11(1):644. 2021-01-12 [PMID: 33436772] (Human) Human
ED Laing, CK Navaratnar, S Cheliout D, SR Petzing, Y Xu, SL Sterling, GA Marsh, LF Wang, M Amaya, DB Nikolov, R Cattaneo, CC Broder, K Xu Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus Proc. Natl. Acad. Sci. U.S.A., 2019-09-23;0(0):. 2019-09-23 [PMID: 31548390] (Coprecipitation Assay, Virus - Henipavirus) Coprecipitation Assay Virus - Henipavirus
Baumer B, Kurz A, Borrie S, Sickinger S, Dours-Zimmermann M, Zimmermann D, Bandtlow C Nogo receptor homolog NgR2 expressed in sensory DRG neurons controls epidermal innervation by interaction with Versican. J Neurosci, 2014-01-29;34(5):1633-46. 2014-01-29 [PMID: 24478347] (Bioassay, Mouse) Bioassay Mouse
Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Hahn AS, Kaufmann JK, Wies E, Naschberger E, Panteleev-Ivlev J, Schmidt K, Holzer A, Schmidt M, Chen J, Konig S, Ensser A, Myoung J, Brockmeyer NH, Sturzl M, Fleckenstein B, Neipel F The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi&#039;s sarcoma-associated herpesvirus. Nat. Med., 2012-06-01;18(6):961-6. 2012-06-01 [PMID: 22635007] (Control, Human) Control Human
Dawson DW, Hong JS, Shen RR, French SW, Troke JJ, Wu YZ, Chen SS, Gui D, Regelson M, Marahrens Y, Morse HC, Said J, Plass C, Teitell MA Global DNA methylation profiling reveals silencing of a secreted form of Epha7 in mouse and human germinal center B-cell lymphomas. Oncogene, 2007-01-29;26(29):4243-52. 2007-01-29 [PMID: 17260020] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol EFNA4
Uniprot