Recombinant Human EphA2 Protein (C-6His)

Name: Recombinant Human EphA2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1247NP
Availability: InStock

BL-1247NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human Ephrin A Receptor 2 is produced by our Mammalian expression system and the target gene encoding Ala24-Asn534 is expressed with a 6His tag at the C-terminus.
Accession	P29317
Synonym	Ephrin type-A receptor 2; Epithelial cell kinase; Tyrosine-protein kinase receptor ECK; EPHA2
Gene Background	EphA2 is a member of the Eph receptor tyrosine kinase family which binds Ephrins A1, 2, 3, 4, and 5. 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. EphA2 becomes autophosphorylated following ligand binding and then interacts with SH2 domain-containing PI3-kinase to activate MAPK pathways. Reverse signaling is also propagated through the Ephrin ligand. Transcription of EphA2 is dependent on the expression of E-Cadherin, and can be induced by p53 family transcription factors. EphA2 is upregulated in breast, prostate, and colon cancer vascular endothelium. Its ligand, EphrinA1, is expressed by the local tumor cells. In some cases, EphA2 and EphrinA1 are expressed on the same blood vessels. EphA2 signaling cooperates with VEGF receptor signaling in promoting endothelial cell migration.
Molecular Mass	57 KDa
Apmol Mass	65-75 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, 5% Trehalose, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 3386 OMIM: 116600 KEGG: hsa:1969 STRING: 9606.ENSP00000351209 UniGene: PMID: 29133884 EphA2 has a role in extracellular vesicle secretion from senescent cells that promote cancer cell proliferation PMID: 28585531 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 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 EphA2 SAM domain inhibits kinase activity by reducing receptor oligomerization. PMID: 28338017 miR-141 inhibits glioma neovascularization by controlling EphA2 expression. PMID: 29901110 when overexpressed, EphA2 induces ERK activation through its tyrosine kinase activity, leading to S897 phosphorylation and promotion of glioblastoma cell proliferation. PMID: 29626472 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 High EPHA2 expression is associated with epithelial-mesenchymal transition in gastric cancer. PMID: 29273006 Ligand-independent activation of EphA2 was triggered by VEGF released from CAF-CM. PMID: 29948146 EphA2-mediates glutaminolysis through YAP/TAZ activation in HER2-positive breast cancer and may serve as potential therapeutic targets in patients. PMID: 29208682 Data indicate a promising role for EPH receptor A2 (EPHA2) as a target in antibody treatments for melanoma. PMID: 29848674 These observations demonstrate that EphA2 affects the sensitivity to oxaliplatin by inducing EMT in oxaliplatin-resistant gastric cancer cells. PMID: 28624791 High erythropoietin-producing hepatocellular carcinoma receptor A (EphA) 1, 2, and 4 expression levels were significantly related to recurrence. PMID: 29491103 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 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 The YSA peptide stabilizes the EphA2 dimer. PMID: 27281300 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 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 The SAM domain inhibits EphA2-ligands interactions in the plasma membrane. PMID: 27776928 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 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 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 EphA2, a member of the large family of Ephrin receptor tyrosine kinases, is a functional signaling receptor for progranulin. PMID: 27903606 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 EphA2 is a key downstream target of the MEK/ERK/RSK signaling pathway in the regulation of glioblastoma cell proliferation. PMID: 27132626 possible involvement of membrane-type 1 matrix metalloproteinase processing of erythropoietin-producing hepatocellular receptor-2in invasiveness of cutaneous cutaneous squamous cell carcinoma PMID: 27056569 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 Data show that the EphA2 ectodomain harbors a membrane-binding motif in the FN2 domain which preferentially interacts with anionic lipids. PMID: 26724997 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 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 These data suggest that miR-26b enhances the radiosensitivity of 97H hepatocellular cancer cells by targeting EphA2 protein. PMID: 26843134 EphA2 protein may be used as a new marker for the prognosis of clear cell renal cell carcinoma. PMID: 26722543 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 EphA2 Expression Is a Key Driver of Migration and Invasion and a Poor Prognostic Marker in Colorectal Cancer PMID: 26283684 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 The present study does not support a major role of EphA2 in cataractogenesis in an Estonian population. PMID: 24673449 Overexpression of Ephrin A2 receptor in cancer stromal cells is a prognostic factor for the relapse of gastric cancer. PMID: 24908114 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 Overexpression of miR-26b dramatically inhibited the proliferation, invasion, and migration of hepatocellular carcinoma cells by targeting EphA2. PMID: 26191168 EphA2/FAK/RhoA signaling pathway plays a critical role in the malignant cellular behavior of renal cell carcinoma PMID: 26177500 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 peptide fragments of Odin-Sam1 interacting with EphA2-Sam PMID: 26120079 we show that EphA2 is an undiscovered important surface and intracellular signaling receptor that is crucial for chlamydial infection and development. PMID: 25906164 SLAP controls SRC/EPHA2/AKT signalling via destabilization of the SRC substrate and receptor tyrosine kinase EPHA2 PMID: 24457997 Ligand-independent EPHA2 signaling drives the adoption of a targeted therapy-mediated metastatic melanoma phenotype PMID: 25542447 EPHA2 is a mediator of vemurafenib resistance and a novel therapeutic target in melanoma PMID: 25542448 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 Data show that ligand-binding domain of receptor tyrosine kinase EphA2 is cleaved frequently by the membrane metalloproteinase MT1-MMP. PMID: 26130649 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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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