Recombinant Human EphA4 Protein

Name: Recombinant Human EphA4 Protein
Brand: Beta LifeScience
SKU: BL-1913NP
Availability: InStock

BL-1913NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Enzymes, Kinase, Recombinant proteins

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Product Overview

Description	Recombinant Human Ephrin type-A Receptor 4 is produced by our Mammalian expression system and the target gene encoding Val20-Thr547 is expressed.
Accession	P54764
Synonym	Ephrin type-A receptor 4;HEK8; SEK; TYRO1;EPHA4;Tyrosine-protein kinase receptor SEK;Tyrosine-protein kinase TYRO1;EK8;hEK8;EPH-like kinase 8
Gene Background	Ephrin type-A receptor 4(EPHA4) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHA4 contains 1 Eph LBD domain, 2 fibronectin type-III domains, 1 protein kinase domain and 1 SAM domain. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.
Molecular Mass	59.2 KDa
Apmol Mass	60-80 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, 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 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	HGNC: 3388 OMIM: 602188 KEGG: hsa:2043 STRING: 9606.ENSP00000281821 UniGene: Hs.371218
Tissue Specificity	Ubiquitous.

Gene Functions References

MiR-519d down-regulates EphA4 expression in melanoma. PMID: 29093007
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
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
These results demonstrate a novel role for SORLA as a physiological and pathological EphA4 modulator. PMID: 29114064
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
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
Molecular interactions of EphA4, growth hormone receptor, Jak2, and STAT5B have been described. PMID: 28686668
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
Reduced EphA4 expression is associated with EBV-associated B lymphoma. PMID: 27338098
No difference was found in the expression of EPHA4 in morphologically normal glands, HGPIN, or prostatic cancer. PMID: 27804940
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
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
Host EphA4 expression regulates cancer development mainly via EphA4-mediated IGF1 synthesis signal. PMID: 26923183
EPHA4 is overexpressed but not functionally active in Sezary syndrome. PMID: 26376612
The signaling complex appears to integrate the input from FGFR and EphA4, and release the output signal through FRS2alpha. PMID: 20184660
EphA4 induced accumulation of amyloid precursor protein through a Lyn-mediated pathway. PMID: 24217950
High Eph A4 expression is associated with choriocarcinoma invasion. PMID: 23429488
The platelet P2Y12 receptor contributes to granule secretion through Ephrin A4 receptor. PMID: 22273509
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
Epha4 modulates the vulnerability of motor neurons to axonal degeneration and may represent a new target for therapeutic intervention in ALS. PMID: 22922411
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
EphA4 expression maintains adult neural stem cells in an undifferentiated state. PMID: 21444754
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
Eph-A4 expression was significantly associated with tumor proliferative capacity in pancreatic ductal adenocarcinoma. PMID: 19949912
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
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
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
FGF-receptor-mediated mitogen-activated protein kinase stimulation is potentiated in cells costimulated with ephrin-A1 PMID: 16365308
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
Overexpression of EphA4 receptor is associated with pancreatic ductal adenocarcinoma PMID: 16965393
overexpression of the EphA4 gene and reduced expression of the EphB2 gene might promote liver metastasis in colorectal cancer PMID: 18695888
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
Overexpression of the receptor tyrosine kinase EphA4 in human gastric cancers. PMID: 18837080

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.