Recombinant Human EphA4 Protein (aa 570-986, His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1807

Recombinant Human EphA4 Protein (aa 570-986, His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1807
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Product Overview

Tag His&GST
Host Species Human
Accession P54764
Synonym HEK8, SEK, TYRO1
Background EPH receptor A4 (ephrin type-A receptor 4), also known as EphA4, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA1, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. EphA4 is enriched on dendritic spines of pyramidal neurons in the adult mouse hippocampus, and ephrin-A3 is localized on astrocytic processes that envelop spines. Eph receptor-mediated signaling, which is triggered by ephrins7, probably modifies the properties of synapses during synaptic activation and remodeling. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). The extracellular domain of an EphA4 interacts with ephrin ligands, which may be tethered to neighbouring cells. Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer.
Description A DNA sequence encoding the human EPHA4 (P54764) (Ser570-Val986) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Ser570-Val986
Molecular Weight The recombinant human EPHA4 /GST chimera consists of 654 a.a. and has a calculated molecular mass of 75 kDa. The recombinant protein migrates as an approximately 67 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. The specific activity was determined to be 17 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate.2. Measured by its binding ability in a functional ELISA. Immobilized human EPHA4 (aa 570-986) at 10 ug/ml (100 ul/well) can bind biotinylated human EphrinA5-His with a linear range of 0.625-5.0 ug/ml.
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, pH 8.5, 10% glycerol, 3mM DTT.
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 membrane-bound ephrin 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. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Cell projection, axon. Cell projection, dendrite. Cell junction, synapse, postsynaptic density membrane. Early endosome. Cell junction, adherens junction.
Protein Families Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
Database References
Tissue Specificity Ubiquitous.

Gene Functions References

  1. MiR-519d down-regulates EphA4 expression in melanoma. PMID: 29093007
  2. These findings confirmed that EphA4 is a direct target gene of miR-335 and that miR-335 suppresses breast cancer cell proliferation and motility in part by directly inhibiting EphA4 expression. PMID: 28795314
  3. Therefore EphA4 is an emerging AbetaOs receptor and the activation of the EphA4/c-Abl axis would explain the synaptic spine alterations found in Alzheimer's disease. PMID: 29378302
  4. These results demonstrate a novel role for SORLA as a physiological and pathological EphA4 modulator. PMID: 29114064
  5. The expression of both EphA4-FL and EphA4-N was significantly higher in the nervous tissue of SOD1(G93A) compared to wild-type mice suggesting that both forms are modulated during the disease process. PMID: 28153688
  6. the PI3K/AKT, Wnt/beta-catenin signaling pathways as well as ERK1/2 downstream of EPHA4 receptor activation, play an important role in the regulation of events related with the EMT development, which may be associated with the therapeutic failure in rectal cancer after radiotherapy. PMID: 27632701
  7. Molecular interactions of EphA4, growth hormone receptor, Jak2, and STAT5B have been described. PMID: 28686668
  8. Findings demonstrated that mutant alpha2-chimaerin and EphA4 have different genetic interactions in distinct motor neuron pools: abducens neurons use bidirectional ephrin signaling via mutant alpha2-chimaerin to direct growth, while cervical spinal neurons use only ephrin forward signaling PMID: 28346224
  9. Reduced EphA4 expression is associated with EBV-associated B lymphoma. PMID: 27338098
  10. No difference was found in the expression of EPHA4 in morphologically normal glands, HGPIN, or prostatic cancer. PMID: 27804940
  11. we supposed that EphA4 interacted with CDK5 and promoted its expression which in turn enhanced p-AKT expression and promoted cell adhesion-mediated drug resistance in multiple myeloma. PMID: 28351297
  12. EphA4 was reduced in breast carcinoma, which is associated with high grade, advanced TNM stage, lymph node metastasis, and poor outcome of patients PMID: 27478038
  13. Host EphA4 expression regulates cancer development mainly via EphA4-mediated IGF1 synthesis signal. PMID: 26923183
  14. EPHA4 is overexpressed but not functionally active in Sezary syndrome. PMID: 26376612
  15. The signaling complex appears to integrate the input from FGFR and EphA4, and release the output signal through FRS2alpha. PMID: 20184660
  16. EphA4 induced accumulation of amyloid precursor protein through a Lyn-mediated pathway. PMID: 24217950
  17. High Eph A4 expression is associated with choriocarcinoma invasion. PMID: 23429488
  18. The platelet P2Y12 receptor contributes to granule secretion through Ephrin A4 receptor. PMID: 22273509
  19. EphA4 gene expression is associated with an improved outcome in patients with resected lung adenocarcinoma, possibly by affecting cancer cell migration and invasion. PMID: 22807579
  20. Epha4 modulates the vulnerability of motor neurons to axonal degeneration and may represent a new target for therapeutic intervention in ALS. PMID: 22922411
  21. The present study demonstrates that EphA4 is expressed on neurons in multiple regions of the intact human brain and is markedly upregulated on activated astrocytes after TBI PMID: 22318127
  22. EphA4 expression maintains adult neural stem cells in an undifferentiated state. PMID: 21444754
  23. these results suggest that the ligand promiscuity of the Ephs is directly correlated with the structural flexibility of the ligand-binding surface of the receptor. PMID: 20678482
  24. Eph-A4 expression was significantly associated with tumor proliferative capacity in pancreatic ductal adenocarcinoma. PMID: 19949912
  25. Eph/ephrin signaling enhances the ability of platelet agonists to cause aggregation provided that those agonists can increase cytosolic Ca(++) and this is accomplished in part by activating Rap1 PMID: 14576067
  26. The tyrosine kinase receptor EphA4 and the potentially oncogenic transcription factor Twist were highly and selectively expressed in T cells of patients with Sezary Syndrome. PMID: 15313894
  27. EphA4 is physically associated with alpha(IIb)beta(3) in resting platelets, increases its surface expression when platelets are activated, and colocalizes with alpha(IIb)beta(3) at sites of contact between platelets. PMID: 15994237
  28. FGF-receptor-mediated mitogen-activated protein kinase stimulation is potentiated in cells costimulated with ephrin-A1 PMID: 16365308
  29. The expression of EphA4 in astrocyte progenitor cells and in the astrocyte meshwork at the optic nerve head has implications for optic nerve pathologies. PMID: 16574431
  30. Overexpression of EphA4 receptor is associated with pancreatic ductal adenocarcinoma PMID: 16965393
  31. overexpression of the EphA4 gene and reduced expression of the EphB2 gene might promote liver metastasis in colorectal cancer PMID: 18695888
  32. These results indicate that EphA4 plays an important role in malignant phenotypes of glioblastoma by enhancing cell proliferation and migration through accelerating a canonical FGFR signaling pathway. PMID: 18790757
  33. Overexpression of the receptor tyrosine kinase EphA4 in human gastric cancers. PMID: 18837080

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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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