Recombinant Human EphA2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1798

Recombinant Human EphA2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1798
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Product Overview

Tag His
Host Species Human
Accession P29317
Background Eph receptor A2 (Ephrin type-A receptor 2 or EphA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. The Eph receptors' corresponding family of ligands are the ephrins anchored to cell surfaces. The ephrins and Eph receptors are implicated as positional labels that may guide the development of neural topographic maps. They have also been found implicated in embryonic patterning, neuronal targeting, vascular development and adult neovascularization. The large family of ligands and receptors may make a major contribution to the accurate spatial patterning of connections and cell position in the nervous system. Furthermore, elevated expression of Eph receptors and ephrin ligands is associated with tumors and associated tumor vasculature, suggesting the Eph receptors and ephrin ligands also play critical roles in tumor angiogenesis and tumor growth. Unlike most Eph kinases, which are primarily expressed during development, EphA2 is primarily found in adult human epithelial cells. The cellular functions of EphA2 may be regulating cell growth, survival, migration, and angiogenesis.Unlike other receptor tyrosine kinases, ligand binding is not necessary for EphA2. Rather, the ligand appears to regulate EphA2 subcellular localization and its interactions with downstream adapter and signaling proteins. Eph receptor A2(EphA2) has been demonstrated to critically regulate tumor cell growth, migration and invasiveness. Eph receptor A2(EphA2) is frequently overexpressed and functionally altered in aggressive tumor cells, and that these changes promote metastatic character.
Description A DNA sequence encoding the human EPHA2 (P29317) (Met1-Asn534) was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Ala 24
AA Sequence Met1-Asn534
Molecular Weight The recombinant human EPHA2 consists of 522 a.a. and predicts a molecular mass of 57.6 KDa. It migrates as an approximately 65-75 KDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its binding ability in a functional ELISA. Immobilized human EPHA2-His at 10 ug/ml (100 ul/well) can bind human EFNA1-Fch, The EC50 of human EFNA1-Fch is 0.1-0.2 ug/ml.
Formulation Lyophilized from sterile 20mM Tris, 150mM NaCl,- pH 7.5..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.; (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane; Single-pass type I membrane protein. Cell projection, lamellipodium membrane; Single-pass type I membrane protein. Cell junction, focal adhesion.
Protein Families Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
Database References
Associated Diseases Cataract 6, multiple types (CTRCT6)
Tissue Specificity Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary.

Gene Functions References

  1. Binding of Candida albicans to ephrin type-A receptor 2 (EphA2) on oral epithelial cells activates signal transducer and activator of transcription 3 and mitogen-activated protein kinase signalling, and is required for induction of a proinflammatory and antifungal response. EphA2 (-/-) mice have impaired inflammatory responses and reduced interleukin-17 signalling during oropharyngeal candidiasis. PMID: 29133884
  2. EphA2 has a role in extracellular vesicle secretion from senescent cells that promote cancer cell proliferation PMID: 28585531
  3. Combination of polymorphisms in the NOD2, IL17RA, EPHA2 and KALRN genes could play a significant role in the development of sarcoidosis by maintaining a chronic pro-inflammatory status in macrophages PMID: 29554915
  4. Phosphorylation of RCP at Ser(435) by Lemur tyrosine kinase-3 (LMTK3) and of EphA2 at Ser(897) by Akt are both necessary to promote Rab14-dependent (and Rab11-independent) trafficking of EphA2 which generates cell:cell repulsion events that drive tumour cells apart. PMID: 28294115
  5. EphA2 SAM domain inhibits kinase activity by reducing receptor oligomerization. PMID: 28338017
  6. miR-141 inhibits glioma neovascularization by controlling EphA2 expression. PMID: 29901110
  7. when overexpressed, EphA2 induces ERK activation through its tyrosine kinase activity, leading to S897 phosphorylation and promotion of glioblastoma cell proliferation. PMID: 29626472
  8. findings suggested inhibition of HDACs-EphA2 signaling axis with WW437 alone or in combination with other agents may be a promising therapeutic strategy for advanced breast cancer. PMID: 29759486
  9. High EPHA2 expression is associated with epithelial-mesenchymal transition in gastric cancer. PMID: 29273006
  10. Ligand-independent activation of EphA2 was triggered by VEGF released from CAF-CM. PMID: 29948146
  11. EphA2-mediates glutaminolysis through YAP/TAZ activation in HER2-positive breast cancer and may serve as potential therapeutic targets in patients. PMID: 29208682
  12. Data indicate a promising role for EPH receptor A2 (EPHA2) as a target in antibody treatments for melanoma. PMID: 29848674
  13. These observations demonstrate that EphA2 affects the sensitivity to oxaliplatin by inducing EMT in oxaliplatin-resistant gastric cancer cells. PMID: 28624791
  14. High erythropoietin-producing hepatocellular carcinoma receptor A (EphA) 1, 2, and 4 expression levels were significantly related to recurrence. PMID: 29491103
  15. the dimer structures of human EphA2 receptor depend on the lipid environment, which we show is linked to the location of the structural motifs in the dimer interface, thereby establishing that both sequence and membrane composition modulate the complete energy landscape of membrane-bound proteins. PMID: 27559086
  16. data suggest that novel germ-line (blood) and somatic (lens) coding SNVs in EPHA2 that are predicted to be functionally deleterious occur in adults over 50 years of age PMID: 29267365
  17. The YSA peptide stabilizes the EphA2 dimer. PMID: 27281300
  18. A 3D structural model of a mutant with a novel 39-AA polypeptide at the C-terminus had partial disorder in the acquired C-terminal tail and a few residues making an alpha-helix and 2 short beta-strands. 2 peptides comprising the whole C-terminus and its predicted helical region, respectively, did not interact with EphA2-Sam or Ship2-Sam. The C-terminus should not wrap the EphA2-Sam End-Helix interface or affect Sam dom... PMID: 28602916
  19. EphA2 expression is enriched in the basal-like breast cancer molecular subtype and correlates with poor recurrence-free survival in human triple-negative breast cancers PMID: 28581527
  20. The SAM domain inhibits EphA2-ligands interactions in the plasma membrane. PMID: 27776928
  21. These findings show that radiation induces S897 EphA2 phosphorylation, an event associated with increased cell survival. Therefore, targeting pathways that mediate EphA2 S897 phosphorylation may be a beneficial strategy to reduce radioresistance. PMID: 28705041
  22. Our findings broaden the spectrum of causative mutations in EPHA2 gene for congenital cataract and suggest that WES is an efficient strategy to scan variants in known causative genes for genetically heterogeneous diseases. PMID: 27380975
  23. Afadin (AFDN), a cytoskeletal and junction-associated protein, was present in 2D and 3D keratinocyte cultures, and validated as a so-far-unknown EphA2-interacting protein. PMID: 27815408
  24. EphA2, a member of the large family of Ephrin receptor tyrosine kinases, is a functional signaling receptor for progranulin. PMID: 27903606
  25. both EphA2 and EphB4 show potential as target for image-guided colorectal cancer surgery, but EphB4 seems to have the best characteristics with respect to tumor/normal mucosa distribution PMID: 28165374
  26. EphA2 is a key downstream target of the MEK/ERK/RSK signaling pathway in the regulation of glioblastoma cell proliferation. PMID: 27132626
  27. possible involvement of membrane-type 1 matrix metalloproteinase processing of erythropoietin-producing hepatocellular receptor-2in invasiveness of cutaneous cutaneous squamous cell carcinoma PMID: 27056569
  28. cells with Lipoplatin. The combined effects of siRNA-EphA2 and Lipoplatin were determined. We report that silencing EphA2 significantly enhanced the cellular sensitivity of lung tumor and MPM cells to Lipoplatin and maybe a potential therapy for lung cancer. PMID: 27438907
  29. Data show that the EphA2 ectodomain harbors a membrane-binding motif in the FN2 domain which preferentially interacts with anionic lipids. PMID: 26724997
  30. Data show that microRNA miR-141 is down-regulated in hepatocellular carcinoma (HCC) tissues and it is negatively correlated with erythropoietin-producing hepatocellular receptor A2 (EphA2) expression. PMID: 27412940
  31. Nuclear expression of EphA2 in this series of large tumours was significantly associated with an increased rate of metastasis. On the other hand, cytoplasmic localisation was associated with a better prognosis. As there was no correlation between EphA2 expression and angiogenesis, the mature vasculature or VM, EphA2 appears to become less important in the advanced stages of the disease. PMID: 26854480
  32. These data suggest that miR-26b enhances the radiosensitivity of 97H hepatocellular cancer cells by targeting EphA2 protein. PMID: 26843134
  33. EphA2 protein may be used as a new marker for the prognosis of clear cell renal cell carcinoma. PMID: 26722543
  34. Mis-localization of two of the mutant proteins in epithelial cells suggests that some disease-causing mutations in EPHA2 likely affect lens epithelial cell homeostasis and contribute to cataract. PMID: 26900323
  35. EphA2 Expression Is a Key Driver of Migration and Invasion and a Poor Prognostic Marker in Colorectal Cancer PMID: 26283684
  36. Based on these findings we propose that EphA2 promotes cell adhesion by an unknown signaling pathway that largely depends on the extracellular region of EphA2 and the activation of outside-in integrin signaling PMID: 26565750
  37. The present study does not support a major role of EphA2 in cataractogenesis in an Estonian population. PMID: 24673449
  38. Overexpression of Ephrin A2 receptor in cancer stromal cells is a prognostic factor for the relapse of gastric cancer. PMID: 24908114
  39. Role for EPHA2 in the maintenance of cell survival of TKI-resistant, EGFR-mutant lung cancer and indicate that EPHA2 may serve as a useful therapeutic target in TKI-resistant tumors. PMID: 26744526
  40. Overexpression of miR-26b dramatically inhibited the proliferation, invasion, and migration of hepatocellular carcinoma cells by targeting EphA2. PMID: 26191168
  41. EphA2/FAK/RhoA signaling pathway plays a critical role in the malignant cellular behavior of renal cell carcinoma PMID: 26177500
  42. EphA2 forms dimers in the plasma membrane of HEK293T cells in the absence of ephrin ligand binding, suggesting that the current seeding mechanism model of EphA2 activation is incomplete. PMID: 26363067
  43. peptide fragments of Odin-Sam1 interacting with EphA2-Sam PMID: 26120079
  44. we show that EphA2 is an undiscovered important surface and intracellular signaling receptor that is crucial for chlamydial infection and development. PMID: 25906164
  45. SLAP controls SRC/EPHA2/AKT signalling via destabilization of the SRC substrate and receptor tyrosine kinase EPHA2 PMID: 24457997
  46. Ligand-independent EPHA2 signaling drives the adoption of a targeted therapy-mediated metastatic melanoma phenotype PMID: 25542447
  47. EPHA2 is a mediator of vemurafenib resistance and a novel therapeutic target in melanoma PMID: 25542448
  48. EPHA2 expression is correlated with poor survival specifically in basal-like breast cancer and its expression is repressed by miR-200a through direct interaction with the 3'UTR of EPHA2. PMID: 26088362
  49. Data show that ligand-binding domain of receptor tyrosine kinase EphA2 is cleaved frequently by the membrane metalloproteinase MT1-MMP. PMID: 26130649
  50. Results show that MiR-26a is overexpressed in patients with atherosclerosis and its role in the disease is mediated by its target EphA2 via a mechanism involving the p38 MAPK/VEGF pathway. PMID: 25613580


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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