Recombinant Rat Ephrin B3 Protein (Fc Tag)

Name: Recombinant Rat Ephrin B3 Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-1882
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Rat
Accession	NP_001094450
Background	Ephrin B3 belongs to the ephrin family. Ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin B3 is important in brain development as well as in its maintenance. It is especially important for forebrain function since its expression levels were particularly high in several forebrain subregions compared to other brain subregions. Ephrin B3 binds to, and induce the collapse of, commissural axons/growth cones in vitro. It may play a role in constraining the orientation of longitudinally projecting axons.
Description	A DNA sequence encoding the rat EFNB3 (NP_001094450) (Met1-Ser224) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Leu 28
AA Sequence	Met1-Ser224
Molecular Weight	The recombinant rat EFNB3/Fc is a disulfide-linked homodimer. The reduced monomer comprises 438 a.a. and has a predicted molecular mass of 48.7 kDa. The apparent molecular mass of the protein is approximately 55 and 34 kDa in SDS-PAGE under reducing conditions.
Purity	(79.6+17)% 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 EphB3-His at 10 ug/ml (100 ul/well) can bind rat EFNB3-Fc, The EC50 of rat EFNB3-Fc is 14.1-33.2 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.