Recombinant Mouse Ephrin A1/EFNA1 Protein

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Mouse
Accession	P52793
Synonym	B61 ECKLG EFL 1 EFL1 EFNA 1 Efna1 EFNA1_HUMAN EPH related receptor tyrosine kinase ligand 1 EPH-related receptor tyrosine kinase ligand 1 Ephrin-A1 Ephrin-A1, secreted form EphrinA1 EPLG 1 EPLG1 Immediate early response protein B61 LERK 1 LERK-1 LERK1 Ligand of eph related kinase 1 OTTHUMP00000033242 OTTHUMP00000033271 secreted form TNF alpha-induced protein 4 TNFAIP 4 TNFAIP4 Tumor necrosis factor alpha induced protein 4 Tumor necrosis factor alpha-induced protein 4
Description	Recombinant Mouse Ephrin A1/EFNA1 Protein was expressed in Mammalian. It is a Full length protein
Source	Mammalian
AA Sequence	DRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYT LYMVEHQEYVACQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGK EFKEGHSYYYISKPIYHQESQCLKLKVTVNGKITHNPQAHVNPQEKRLQA DDPEVQVLHSIGYSVDDIEGRMDEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQ PREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK TTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLS LSPGKHHHHHH
Molecular Weight	47 kDa including tags
Purity	>95% SDS-PAGE.Purity is determined by SEC-HPLC and reducing SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. The lyo

Target Details

Target Function	Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor.; [Ephrin-A1, secreted form]: Secreted.
Protein Families	Ephrin family
Database References	KEGG: mmu:13636 STRING: 10090.ENSMUSP00000029566 UniGene: Mm.15675
Tissue Specificity	Expressed in myogenic progenitor cells.

Gene Functions References

EphA2 mAb treatment could partially inhibit LPSinduced inactivation of EphBEphrin B3 signalling, while Ephrin B3 overexpression could abrogate LPSinduced activation of EphA2Ephrin A1 signalling. EphB1/Ephrin B3 signalling may antagonise the EphA2/Ephrin A1dependent pathway following LPS treatment. PMID: 29901151
Collectively, these data suggest that ATRA attenuates bleomycin-induced pulmonary fibrosis by regulating EphA2-EphrinA1 and PI3K-Akt signaling. PMID: 28743499
Lipopolysaccharide exposure significantly up-regulated EphA2 and EphrinA1 expression. PMID: 27549114
Activation of EphA1-Epha receptor axis attenuates diabetic nephropathy in mice. PMID: 28341121
Following ephrin-A1 stimulation, truncated EphA2 did not detectably interfere with the phosphorylation of endogenous EphA2, and it potentiated cell adhesion possibly through modulation of integrin avidity. PMID: 27665280
ADAM12 enhanced ephrin-A1 cleavage in response to transforming growth factor-betra1 in primary tumors. PMID: 23686306
S100A8 and ephrin-A1 contribute to lung metastasis. PMID: 24103748
We used in utero electroporation-mediated EphA7 overexpression in developing somatosensory corticothalamic axons to dissect EphA7/ephrin-A-dependent mechanisms involved in regulating both initial targeting and postnatal growth of the CT projections. PMID: 22821544
Elevated levels of ephrin-A1 may contribute to diabetic keratopathies by persistently engaging EphA2 and prohibiting Akt-dependent corneal epithelial repair processes. PMID: 22247486
Data indicate that ephrin-A1 regulates cardiac valve development, making ephrin-A1-deficient mice a novel model for congenital heart defects. PMID: 20960543
Cooperation between Slit2 and ephrin-A1 regulates a balance between the pro- and antiangiogenic functions of Slit2. PMID: 21135133
ephrin-A1 has a positive role in tumor growth in vivo, and are consistent with previous reports of ephrin-A1 acting through EphA receptors in the tumor microenvironment in vivo. PMID: 20154726
When NIH3T3 cells were plated onto an ephrinA1-coated surface, the cells both adhered and spread. PMID: 12134157
Immunohistological analyses reveal strong ephrin-A1 expression in lung tissue, low expression in cortical areas of lymph nodes, and none in T cell/B cell areas of the spleen. PMID: 14707054
Whole-mount in situ hybridization revealed overlapping expression of the Epha1 receptor and its high-affinity ligands ephrin A1 (Efna1) and ephrin A3 (Efna3) in the primitive streak and the posterior paraxial mesoderm during early mouse development. PMID: 16466970
Ephrins A1 and A5 are substrates for a cross-linking enzyme, tissue transglutaminase, which mediates the formation of oligomeric ephrin. PMID: 17707797
Increased expression of ephrin-A1 accelerated the malignant progression of the intestinal adenoma to invasive tumors. PMID: 18246128
HIF-2alpha plays an essential role in vascular remodeling during tumor vascularization through activation of at least ephrin A1. PMID: 18434321
Radiotherapy-induced changes in ephrin-A1 gene expression related with angiogenesis may modulate microenvironment and influence responsiveness of tumors. PMID: 18997097

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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.