Recombinant Human Ephrin-A5 (EFNA5) Protein (hFc), Active

Name: Recombinant Human Ephrin-A5 (EFNA5) Protein (hFc), Active
Brand: Beta LifeScience
SKU: BLC-05579P
Price: 349.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Activity Measured by its binding ability in a functional ELISA. Immobilized EPHA3 at 2 μg/ml can bind human EFNA5, the EC 50 of human EFNA5 protein is 0.8674-1.119 ng/ml. Biological Activity Assay

Activity Human EPHA3 protein his tag captured on COOH chip can bind Human EFNA5 protein Fc tag with an affinity constant of 13.8 nM as detected by LSPR Assay. Biological Activity Assay

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Price Save $58

Size

100ug

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Product Overview

Description	Recombinant Human Ephrin-A5 (EFNA5) Protein (hFc), Active is produced by our Mammalian cell expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/ug as determined by LAL method.
Activity	1. Measured by its binding ability in a functional ELISA. Immobilized EPHA3 at 2 μg/ml can bind human EFNA5, the EC50 of human EFNA5 protein is 0.8674-1.119 ng/ml. 2. Human EPHA3 protein his tag captured on COOH chip can bind Human EFNA5 protein Fc tag with an affinity constant of 13.8 nM as detected by LSPR Assay.
Uniprotkb	P52803
Target Symbol	EFNA5
Synonyms	EPLG7; AF1; AL 1; AL-1; EFL5; Efna5; EFNA5_HUMAN; EPH-related receptor tyrosine kinase ligand 7; Ephrin A5; Ephrin-A5; EPLG7; GLC1M; LERK-7; LERK7; RAGS
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc
Target Protein Sequence	QDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGEN
Expression Range	21-203aa
Protein Length	Full Length of Mature Protein
Mol. Weight	50.1 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, pH 7.4
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. 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

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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.