Recombinant Rat EphA3 Protein (His Tag)

Name: Recombinant Rat EphA3 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1806
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Enzymes, Kinase, Recombinant proteins

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Product Overview

Tag	His
Host Species	Rat
Accession	G3V9D6
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 rat EPHA3 (EDL75897.1) (Met1-His541) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Glu 21
AA Sequence	Met1-His541
Molecular Weight	The recombinant rat EPHA3 comprises 532 a.a. and predicts a molecular mass of 61.2 kDa. The apparent molecular mass of the recombinant protein is approximately 70.5 kDa in SDS-PAGE under reducing conditions due to glycosylation.
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 rat EPHA3-His at 10 ug/ml (100 ul /well) can bind rat EFNA5-Fc, The EC50 of ratEFNA5-Fc is 9-20ng/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.