Recombinant Human EFNA5 Protein (C-Fc)

Name: Recombinant Human EFNA5 Protein (C-Fc)
Brand: Beta LifeScience
SKU: BL-0099NP
Availability: InStock

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ephrin-A5 is produced by our Mammalian expression system and the target gene encoding Gln21-Asn203 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession	P52803
Synonym	Ephrin-A5;EPLG7; LERK7;EFNA5;LERK-7;EPH-related receptor tyrosine kinase ligand 7;AL-1
Gene Background	Ephrin-A5 (EFNA5) belongs to the ephrin family,contains 1 ephrin RBD (ephrin receptor-binding) domain. Ephrin-A5 is a 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. It binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
Molecular Mass	48.3 KDa
Apmol Mass	55-60 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
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. 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor. Membrane, caveola; Lipid-anchor, GPI-anchor. Note=Compartmentalized in discrete caveolae-like membrane microdomains.
Protein Families	Ephrin family
Database References	HGNC: 3225 OMIM: 601535 KEGG: hsa:1946 STRING: 9606.ENSP00000328777 UniGene: Hs.288741

Gene Functions References

These results indicate a novel mechanism of ephrin-Eph signaling independent of direct cell contact and proteolytic cleavage and suggest the participation of EphB2(+) extracellular vesicles in neural development and synapse physiology. PMID: 27354374
MiR-96 and miR-182 are upregulated in hepatocellular carcinoma and negatively associated with ephrin A5 expression. PMID: 25663355
the structure of the ligand-binding domain of the EphA3 receptor in complex with its preferred ligand, ephrin-A5, is reported. PMID: 25993310
The genetic variations c.668C>T (rs201008479), c.102C>T (rs199980747) and c.-27C>G (rs200187971) may present an additional genetic risk factor for age-related cataract in the Chinese population. PMID: 25300504
Data indicate that ephrin-A5 binding directly facilitates the formation of Eph/ephrin clusters by inducing conformational changes in the ligand-binding domain (LBD) of EphA4. PMID: 23959867
Transgenic ephrin-A5 plays a critical role in postnatal lens fiber organization to maintain lens transparency: cells in the ephrin-A5-deficient lens are severely disorganized PMID: 23401654
EphrinA5, especially ephrinA5S, acts as a tumor suppressor in hepatocarcinogenesis. PMID: 22860012
This study presented that EFNA5 showed strong associations with alcohol withdrawal symptoms. PMID: 22072270
Data suggest that ephrinA5 mRNA/protein levels are reduced in colon adenocarcinoma compared to normal colon tissue; staging/grading indicates that ephrinA5 inhibits colon adenocarcinoma progression via c-Cbl-mediated EGFR ubiquitination/degradation. PMID: 22074469
ephrin-A5-induced cell-morphologic changes of EphA3-positive LK63 pre-B acute lymphoblastic leukemia cells PMID: 18385452
These observations indicate that only a subset of signal transduction pathways is required for ephrin-A5-induced growth cone collapse. PMID: 18563700
ephrinA5 acted as a tumor suppressor in glioma, and its negative regulation of EGFR contributed to the suppressive effects. PMID: 19270726
EFNA5 down-regulation is a consistent finding in chondrosarcomas PMID: 19695673

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.