Recombinant Mouse EFNA1 Protein (C-Fc-6His)

Name: Recombinant Mouse EFNA1 Protein (C-Fc-6His)
Brand: Beta LifeScience
SKU: BL-2376NP
Availability: InStock

BL-2376NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Ephrin-A1 is produced by our Mammalian expression system and the target gene encoding Asp19-Ser182 is expressed with a human IgG1 Fc, 6His tag at the C-terminus.
Accession	P52793
Synonym	EPH-related receptor tyrosine kinase ligand 1; Immediate early response protein B61;Epgl1; Epl1; Lerk1
Gene Background	Ephrin-A1 is a cell membrane protein and contains 1 ephrin RBD (ephrin receptor-binding) domain. EFNA1 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.It belongs to the ephrin family and contains 1 ephrin RBD (ephrin receptor-binding) domain.
Molecular Mass	47.3 KDa
Apmol Mass	45-65 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 90% 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	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

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.