Recombinant Human EPT1 Protein (N-GST)

Name: Recombinant Human EPT1 Protein (N-GST)
Brand: Beta LifeScience
SKU: BL-0265NP
Availability: InStock

BL-0265NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Ethanolaminephosphotransferase 1 is produced by our E.coli expression system and the target gene encoding Met1-Pro50 is expressed with a GST tag at the N-terminus.
Accession	Q9C0D9
Synonym	Ethanolaminephosphotransferase 1; hEPT1; Selenoprotein I; SelI; EPT1; KIAA1724; SELI
Gene Background	Ethanolaminephosphotransferase 1 (EPT1) is an enzyme that belongs to the CDP-Alcohol Phosphatidyltransferase Class-I Family. EPT1 is a Selenoprotein, which contains a Selenocysteine (Sec) residue at its active site. The Selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of Selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. EPT1 catalyzes Phosphatidylethanolamine biosynthesis from CDP-Ethanolamine. It plays a central role in the formation and maintenance of vesicular membranes. EPT1 is involved in the formation of Phosphatidylethanolamine via the 'Kennedy' pathway.
Molecular Mass	32.6 KDa
Apmol Mass	29 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM EDTA, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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.