Recombinant Human Ephrin-A1 Fc Chimera Protein, CF

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Recombinant Human Ephrin-A1 Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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.
Mouse myeloma cell line, NS0-derived human Ephrin-A1 protein
Human Ephrin-A1
Accession # P20827
N-terminus C-terminus
Accession #
N-terminal Sequence
Predicted Molecular Mass
46 kDa (monomer)
55-60 kDa, reducing conditions

Product Datasheets

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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.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in 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.
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Background: Ephrin-A1

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.
Entrez Gene IDs
1942 (Human); 13636 (Mouse)
Alternate Names
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

Citations for Recombinant Human Ephrin-A1 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.

16 Citations: Showing 1 - 10
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  1. Aggressive and recurrent ovarian cancers upregulate ephrinA5, a non-canonical effector of EphA2 signaling duality
    Authors: J Jukonen, L Moyano-Gal, K Höpfner, EA Pietilä, L Lehtinen, K Huhtinen, E Gucciardo, J Hynninen, S Hietanen, S Grénman, PM Ojala, O Carpén, K Lehti
    Scientific Reports, 2021;11(1):8856.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Replicating infant-specific reactive astrocyte functions in the injured adult brain
    Authors: L Teo, AG Boghdadi, J Homman-Lud, IC Mundinano, WC Kwan, JA Bourne
    Progress in neurobiology, 2021;0(0):102108.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  3. Targeting EphA2 suppresses hepatocellular carcinoma initiation and progression by dual inhibition of JAK1/STAT3 and AKT signaling
    Authors: H Wang, W Hou, A Perera, C Bettler, JR Beach, X Ding, J Li, MF Denning, A Dhanarajan, SJ Cotler, C Joyce, J Yin, F Ahmed, LR Roberts, W Qiu
    Cell Reports, 2021;34(8):108765.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. C1GALT1 is associated with poor survival and promotes soluble Ephrin A1-mediated cell migration through activation of EPHA2 in gastric cancer
    Authors: PC Lee, ST Chen, TC Kuo, TC Lin, MC Lin, J Huang, JS Hung, CL Hsu, HF Juan, PH Lee, MC Huang
    Oncogene, 2020;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  5. Inhibition of Tumor VEGFR2 Induces Serine 897 EphA2-Dependent Tumor Cell Invasion and Metastasis in NSCLC
    Authors: C Volz, S Breid, C Selenz, A Zaplatina, K Golfmann, L Meder, F Dietlein, S Borchmann, S Chatterjee, M Siobal, J Schöttle, A Florin, M Koker, M Nill, L Ozreti?, N Uhlenbrock, S Smith, R Büttner, H Miao, B Wang, HC Reinhardt, D Rauh, M Hallek, A Acker-Palm, LC Heukamp, RT Ullrich
    Cell Rep, 2020;31(4):107568.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Inhibition of angiogenesis by leflunomide via targeting the soluble ephrin-A1/EphA2 system in bladder cancer
    Authors: M Chu, C Zhang
    Sci Rep, 2018;8(1):1539.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Identification of new EphA4 inhibitors by virtual screening of FDA-approved drugs
    Authors: S Gu, WY Fu, AKY Fu, EPS Tong, FCF Ip, X Huang, NY Ip
    Sci Rep, 2018;8(1):7377.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  8. EPH receptor A2 governs a feedback loop that activates Wnt/?-catenin signaling in gastric cancer
    Authors: Q Peng, L Chen, W Wu, J Wang, X Zheng, Z Chen, Q Jiang, J Han, L Wei, L Wang, J Huang, J Ma
    Cell Death Dis, 2018;9(12):1146.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Ephrin-A1-EphA4 signaling negatively regulates myelination in the central nervous system
    Authors: M Harboe, J Torvund-Je, K Kjaer-Sore, LS Laursen
    Glia, 2018;0(0):.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  10. EphA receptors and ephrin-A ligands are upregulated by monocytic differentiation/maturation and promote cell adhesion and protrusion formation in HL60 monocytes
    Authors: M Mukai, N Suruga, N Saeki, K Ogawa
    BMC Cell Biol., 2017;18(1):28.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. A Modified Adenovirus Vector-Mediated Antibody Screening Method Identifies EphA2 as a Cancer Target
    Authors: T Tanaka, H Yamada, M Kuroki, S Kodama, K Tamura, Y Takamatsu
    Transl Oncol, 2017;10(4):476-484.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  12. Targeting EphA2 impairs cell cycle progression and growth of basal-like/triple-negative breast cancers
    Authors: W Song, Y Hwang, VM Youngblood, RS Cook, JM Balko, J Chen, DM Brantley-S
    Oncogene, 2017;0(0):.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  13. 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.
    Authors: Lennon F, Mirzapoiazova T, Mambetsariev N, Mambetsariev B, Salgia R, Singleton P
    J Biol Chem, 2014;289(35):24043-58.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  14. EphA2 cleavage by MT1-MMP triggers single cancer cell invasion via homotypic cell repulsion.
    Authors: Sugiyama N, Gucciardo E, Tatti O, Varjosalo M, Hyytiainen M, Gstaiger M, Lehti K
    J Cell Biol, 2013;201(3):467-84.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  15. Alteration of the EphA2/Ephrin-A signaling axis in psoriatic epidermis.
    Authors: Gordon K, Kochkodan J, Blatt H, Lin S, Kaplan N, Johnston A, Swindell W, Hoover P, Schlosser B, Elder J, Gudjonsson J, Getsios S
    J Invest Dermatol, 2013;133(3):712-22.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  16. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: 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
    Nature, 2012;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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