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Manufactured by BioVendor

Ephrin Type-A Receptor 2 Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:EphA2, Epithelial cell kinase, ECK, Tyrosine-protein kinase receptor ECK
  • Species:Human
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Cat. No. Size Price

RD172430100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 515 AA. MW: 56.9 kDa (calculated). UniProtKB acc. No. P29317 (Ala24–Glu530). C-terminal linker (2 extra AA) and C-terminal His-tag (6 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence





Purity as determined by densitometric image analysis: > 95 %


12 % SDS-PAGE separation of Human EphA2 (HEK):
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. Reduced and boiled sample, 2.5 μg/lane
3. Non-reduced and non-boiled sample, 2.5 μg/lane


< 0.1 EU/μg


Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in phosphate buffered saline+5 % (w/v) trehalose.


Add 200 µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.


Western blotting, ELISA, Cell culture and/or animal studies


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic



Ephrin Type-A receptor 2 (EphA2 receptor, ECK, ARCC2, Epithelial cell kinase) is a transmembrane glycoprotein composed of 976 amino acid residues, with a calculated molecular mass of 130 kDa. It is one member of the largest EPH (erythropoietin-producing hepatoma amplified sequence) family receptor tyrosine kinases. The ligands for the EPH receptors are ephrins, which consist of 9 members that fall into 2 subclasses: the GPI (glycosylphos­phatidylinosi­tol) anchored A-class of ligands (Ephrin A1–6) and the transmembrane B-class of ligands (B1–3). Receptor tyrosine kinases of the Eph family and Ephrin ligands play important roles in vascular development, tissue-border formation, cell migration, axon guidance and angiogenesis. EphA2 is largely restricted at low levels on adult proliferating epithelial cells and enriched within sites of cell-cell adhesion in normal epithelial cells. EphA2 expression has been detected in a wide assortment of tissues including the brain, skin, bone marrow, lung, thymus, small intestine, colon, urinary bladder, kidney, liver, spleen, uterus, testis and prostate. EphA2 is also expressed during gastrulation in the ectodermal cells and early embryogenesis in the developing hind brain. EphA2 plays key roles in several developmental processes. Recent studies indicate that EphA2 regulates lens transparency, kidney repair following renal injury, bone remodeling, mammary gland branch morphogenesis, and inner ear development, as well as cell transformation in a variety of tumors. The EphA2 protein was overexpressed in the glioblastoma multiforme (GBM) and anaplastic astrocytoma tissues and was identified as a novel target for the development of glioma vaccines. Recent study demonstrates that expression of EphA2 was correlated with decreased differentiation of hepatocellular carcinoma (HCC), making it a useful molecular marker for HCC progression. Overexpression of EphA2 has been found in a wide array of solid tumors, including breast cancer, prostate cancer, colorectal cancer, ovarian cancer, urinary bladder cancer, non-small cell lung cancer, gastric cancer, squamous cervical carcinoma, esophageal squamous cell carcinoma, and melanoma. Overexpression of EphA2 is significantly associated with cancer progression, metastasis and shorter overall survival in cancers. EphA2 is proposed to be an oncogene and a potential target for cancer therapy.

Summary References (11)

References to Ephrin Type-A Receptor 2

  • Abraham S, Knapp DW, Cheng L, Snyder PW, Mittal SK, Bangari DS, Kinch M, Wu L, Dhariwal J, Mohammed SI. Expression of EphA2 and Ephrin A-1 in carcinoma of the urinary bladder. Clin Cancer Res. 2006 Jan 15;12 (2):353-60
  • Chakraborty S, Veettil MV, Bottero V, Chandran B. Kaposi's sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection. Proc Natl Acad Sci U S A. 2012 May 8;109 (19):E1163-72
  • Cui XD, Lee MJ, Yu GR, Kim IH, Yu HC, Song EY, Kim DG. EFNA1 ligand and its receptor EphA2: potential biomarkers for hepatocellular carcinoma. Int J Cancer. 2010 Feb 15;126 (4):940-9
  • Eustace AJ, Kennedy S, Larkin AM, Mahgoub T, Tryfonopoulos D, O'Driscoll L, Clynes M, Crown J, O'Donovan N. Predictive biomarkers for dasatinib treatment in melanoma. Oncoscience. 2014;1 (2):158-66
  • Ferluga S, Hantgan R, Goldgur Y, Himanen JP, Nikolov DB, Debinski W. Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase. J Biol Chem. 2013 Jun 21;288 (25):18448-57
  • Kinch MS, Moore MB, Harpole DH Jr. Predictive value of the EphA2 receptor tyrosine kinase in lung cancer recurrence and survival. Clin Cancer Res. 2003 Feb;9 (2):613-8
  • Merritt WM, Kamat AA, Hwang JY, Bottsford-Miller J, Lu C, Lin YG, Coffey D, Spannuth WA, Nugent E, Han LY, Landen CN, Nick AM, Stone RL, Coffman K, Bruckheimer E, Broaddus RR, Gershenson DM, Coleman RL, Sood AK. Clinical and biological impact of EphA2 overexpression and angiogenesis in endometrial cancer. Cancer Biol Ther. 2010 Dec 15;10 (12):1306-14
  • Park JE, Son AI, Zhou R. Roles of EphA2 in Development and Disease. Genes (Basel). 2013;4 (3):334-57
  • Tandon M, Vemula SV, Mittal SK. Emerging strategies for EphA2 receptor targeting for cancer therapeutics. Expert Opin Ther Targets. 2011 Jan;15 (1):31-51
  • Wang L, Hu H, Tian F, Zhou W, Zhou S, Wang J. Expression of EphA2 protein is positively associated with age, tumor size and Fuhrman nuclear grade in clear cell renal cell carcinomas. Int J Clin Exp Pathol. 2015;8 (10):13374-80
  • Wang LF, Fokas E, Bieker M, Rose F, Rexin P, Zhu Y, Pagenstecher A, Engenhart-Cabillic R, An HX. Increased expression of EphA2 correlates with adverse outcome in primary and recurrent glioblastoma multiforme patients. Oncol Rep. 2008 Jan;19 (1):151-6
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