Recombinant Human EphB4 Protein (aa 563-987, His & GST Tag)

Name: Recombinant Human EphB4 Protein (aa 563-987, His & GST Tag)
Brand: Beta LifeScience
SKU: BLPSN-1840
Availability: InStock

Collections: Enzymes, Kinase, Recombinant proteins

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Product Overview

Tag	His&GST
Host Species	Human
Accession	P54760
Synonym	HTK, MYK1, TYRO11
Background	Ephrin type-B receptor 4 is a protein that in humans is encoded by the EPHB4 gene. It is a single-pass type I membrane protein belonging to the ephrin receptor subfamily of protein kinase superfamily. Members of the ephrin and Eph family are local mediators of cell function through largely contact-dependent processes in development and in maturity. Furthermore, EphB4 protein and the corresponding ligand Ephrin-B2 contribute to tumor growth in various human tumors. EphB4 protein has tumor suppressor activities and that regulation of cell proliferation, extracellular matrix remodeling, and invasive potential are important mechanisms of tumor suppression. Therefore, Ephrin-B2/EphB4 may be recognized as a novel prognostic indicator for cancers.
Description	A DNA sequence encoding the human EPHB4 (P54760) (Leu563-Tyr987) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Leu563-Tyr987
Molecular Weight	The recombinant human EPHB4/GST chimera consists of 662 a.a. and has a calculated molecular mass of 75.2 kDa. The recombinant protein migrates as an approximately 66 kDa band 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	The specific activity was determined to be 47 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate.
Formulation	Supplied as sterile 20mM Tris, 500mM NaCl, pH 8.0, 3mM DTT, 10% gly.
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.