Recombinant Human Ephrin-A1 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Ephrin-A1 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human (rh) EphA2 (Catalog # 3035-A2) is coated at 2 μg/mL (100 μL/well), the concentration of rhEphrin-A1 Fc Chimera that produces 50% of the optimal binding response is found to be approximately 0.6-3 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-A1 protein
Human Ephrin-A1
(Met1-Ser182)
Accession # P20827
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asp19
Protein/Peptide Type
Recombinant Proteins
Gene
EFNA1
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
46 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
55-60 kDa, reducing conditions
Publications
Read Publications using
6417-A1 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
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human Ephrin-A1 Fc Chimera Protein, CF

  • B61
  • ECKLG
  • EFL1
  • EFL-1
  • EFNA1
  • EPH-related receptor tyrosine kinase ligand 1
  • EphrinA1
  • Ephrin-A1
  • EPLG1TNF alpha-induced protein 4
  • Immediate early response protein B61
  • LERK1
  • LERK1LERK-1
  • ligand of eph-related kinase 1
  • TNFAIP4B61
  • Tumor necrosis factor alpha-induced protein 4
  • tumor necrosis factor, alpha-induced protein 4

Background

Ephrin-A1, also known as B61 and LERK-1, is a member of the Ephrin-A family of GPI-anchored ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. Ephrin-A ligands are structurally related to the extracellular domains of the transmembrane Ephrin-B ligands. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). Human Ephrin-A1 is synthesized with an 18 amino acid (aa) signal peptide, a 164 aa mature chain, and a 23 aa C‑terminal propeptide which is removed prior to GPI linkage of Ephrin-A1 to the membrane (3, 4). It can also be released as a soluble molecule (3, 5, 6). The mature 21 ‑ 25 kDa human Ephrin-A1 shares 85% aa sequence identity with mouse and rat Ephrin-A1. Alternate splicing generates an additional isoform that lacks 22 aa in the juxtamembrane region (7).
This short isoform is also expressed on the cell surface and exhibits weakened binding to EphA2 (7). Ephrin-A1 is widely expressed on endothelial and epithelial cells, particularly in the lung, intestine, liver, and skin (4, 8). It is expressed on resting CD4+ T cells but is down‑regulated following activation (9, 10). Ligation of Ephrin-A1 on CD4+ T cells inhibits cell proliferation and activation, although soluble Ephrin-A1 can promote T cell chemotaxis (9, 10). In cancer, Ephrin-A1 is expressed by tumor cells as well as on the tumor‑associated vasculature (5, 6, 11). It inhibits tumor cell proliferation and migration but also supports tumor growth by promoting angiogenesis (12 ‑ 14). Soluble Ephrin-A1 additionally promotes neuronal survival and neurite extension (15).

  1. Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
  2. Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
  3. Holzman, L.B. et al. (1990) Mol. Cell. Biol. 10:5830.
  4. Shao, H. et al. (1995) J. Biol. Chem. 270:5636.
  5. Easty, D.J. et al. (1995) Cancer Res. 55:2528.
  6. Cui, X.-D. et al. (2010) Int. J. Cancer 126:940.
  7. Finne, E.F. et al. (2004) Biochem. J. 379:39.
  8. Takahashi, H. and T. Ikeda (1995) Oncogene 11:879.
  9. Wohlfahrt, J.G. et al. (2004) J. Immunol. 172:843.
  10. Aasheim, H.-C. et al. (2005) Blood 105:2869.
  11. Ogawa, K. et al. (2000) Oncogene 19:6043.
  12. Liu, D.-P. et al. (2007) Int. J. Oncol. 30:865.
  13. Brantley-Sieders, D.M. et al. (2006) Cancer Res. 66:10315.
  14. Pandey, A. et al. (1995) Science 268:567.
  15. Magal, E. et al. (1996) J. Neurosci. Res. 43:735.

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Publications for Ephrin-A1 (6417-A1)(8)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


Filter By Application
Bioassay
(8)
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Filter By Species
Human
(8)
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Showing Publications 1 - 8 of 8.
Publications using 6417-A1 Applications Species
M Chu, C Zhang Inhibition of angiogenesis by leflunomide via targeting the soluble ephrin-A1/EphA2 system in bladder cancer Sci Rep, 2018;8(1):1539. 2018 [PMID: 29367676] (Bioassay, Human) Bioassay Human
M Mukai, N Suruga, N Saeki, K Ogawa EphA receptors and ephrin-A ligands are upregulated by monocytic differentiation/maturation and promote cell adhesion and protrusion formation in HL60 monocytes BMC Cell Biol., 2017;18(1):28. 2017 [PMID: 28851287] (Bioassay, Human) Bioassay Human
W Song, Y Hwang, VM Youngblood, RS Cook, JM Balko, J Chen, DM Brantley-S Targeting EphA2 impairs cell cycle progression and growth of basal-like/triple-negative breast cancers Oncogene, 2017;0(0):. 2017 [PMID: 28581527] (Bioassay, Human) Bioassay Human
T Tanaka, H Yamada, M Kuroki, S Kodama, K Tamura, Y Takamatsu A Modified Adenovirus Vector-Mediated Antibody Screening Method Identifies EphA2 as a Cancer Target Transl Oncol, 2017;10(4):476-484. 2017 [PMID: 28505517] (Bioassay, Human) Bioassay Human
Lennon F, Mirzapoiazova T, Mambetsariev N, Mambetsariev B, Salgia R, Singleton P Transactivation of the receptor-tyrosine kinase ephrin receptor A2 is required for the low molecular weight hyaluronan-mediated angiogenesis that is implicated in tumor progression. J Biol Chem, 2014;289(35):24043-58. 2014 [PMID: 25023279] (Bioassay, Human) Bioassay Human
Sugiyama N, Gucciardo E, Tatti O, Varjosalo M, Hyytiainen M, Gstaiger M, Lehti K EphA2 cleavage by MT1-MMP triggers single cancer cell invasion via homotypic cell repulsion. J Cell Biol, 2013;201(3):467-84. 2013 [PMID: 23629968] (Bioassay, Human) Bioassay Human
Gordon K, Kochkodan J, Blatt H, Lin S, Kaplan N, Johnston A, Swindell W, Hoover P, Schlosser B, Elder J, Gudjonsson J, Getsios S Alteration of the EphA2/Ephrin-A signaling axis in psoriatic epidermis. J Invest Dermatol, 2013;133(3):712-22. 2013 [PMID: 23190894] (Bioassay, Human) Bioassay Human
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;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol EFNA1
Entrez
Uniprot