Recombinant Mouse EphA3 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1803

Recombinant Mouse EphA3 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1803
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.

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Product Overview

Tag Fc
Host Species Mouse
Accession NP_034270.1
Synonym AW492086, Cek4, End3, ETK1, Hek, Hek4, Mek4, Tyro4
Background EPHA3 gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA3 gene encodes a protein that binds ephrin-A ligands. EPHA3 is involved in the retinotectal mapping of neurons. It may also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description A DNA sequence encoding the extracellular domain of mouse EPHA3 (NP_034270.1)(Met1-His541) was expressed with the Fc region of human IgG1 at the C-terminus.
Source HEK293
Predicted N Terminal Glu 21
AA Sequence Met1-His541
Molecular Weight The recombinant mouse EPHA3/Fc comprises 762 a.a. and has a predicted molecular mass of 85.7 kDa. The apparent molecular mass of the protein is approximately 96 kDa in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its binding ability in a functional ELISA.Immobilized mouse EFNA5-His at 10 ug/ml (100 ul/well) can bind mouse EPHA3-Fc, The EC50 of rat mouse EPHA3-Fc is 12.3-28.9 ng/ml.
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.

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