Recombinant Mouse Ephrin-A1 (EFNA1) Protein (His-hFc), Active

Name: Recombinant Mouse Ephrin-A1 (EFNA1) Protein (His-hFc), Active
Brand: Beta LifeScience
SKU: BLC-05871P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Ephrin-A1 (EFNA1) Protein (His-hFc), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by its ability to bind Human EphA2 in functional ELISA is less than 20 ug/ml.
Uniprotkb	P52793
Target Symbol	EFNA1
Synonyms	Efna1; Epgl1; Epl1; Lerk1; Ephrin-A1; EPH-related receptor tyrosine kinase ligand 1; LERK-1; Immediate early response protein B61) [Cleaved into: Ephrin-A1; secreted form]
Species	Mus musculus (Mouse)
Expression System	Mammalian cell
Tag	C-6His-hFc
Complete Sequence	DRHIVFWNSSNPKFREEDYTVHVQLNDYLDIICPHYEDDSVADAAMERYTLYMVEHQEYVACQPQSKDQVRWNCNRPSAKHGPEKLSEKFQRFTPFILGKEFKEGHSYYYISKPIYHQESQCLKLKVTVNGKITHNPQAHVNPQEKRLQADDPEVQVLHSIGYS
Expression Range	19-182aa
Protein Length	Partial
Mol. Weight	47.3 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.