Recombinant Human ENTPD2 Protein (aa 29-460, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1770

Recombinant Human ENTPD2 Protein (aa 29-460, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1770
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Product Overview

Tag His
Host Species Human
Accession Q9Y5L3
Synonym CD39L1, NTPDase-2, RP11-229P13.11-001
Background NTPDase 2, also known as ENTPD2, belongs to the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). Members of E-NTPDase family are nucleotidases able to hydrolyze 5-€²-nucleoside tri- and/or diphosphates; the main role of these enzymes is the termination of purinergic signaling. NTPDases are ubiquitous and were previously shown in other parasites including the trypanosomatides of genus Leishmania and in T. brucei. NTPase activity would act as a timer and is crucial to T. gondii infection. In L. pneumophila it was demonstrated that an E-NTPDase, similar to CD39, is essential for intracellular bacterial multiplication. NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Alternative splicing of NTPDase 2 gene results in multiple transcript variants.
Description A DNA sequence encoding the mature form of human ENTPD2 (Q9Y5L3) (Thr29-Asp460) was expressed, with a His tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal His
AA Sequence Thr29-Asp460
Molecular Weight The recombinant human human ENTPD2 consists of 448 a.a. and predicts a molecular mass of 49.3 KDa. It migrates as an approximately 59 KDa band in SDS-PAGE under reducing conditions.
Purity >85% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to hydrolyze the 5-€™phosphate groups from the substrate adenosine 5-€™triphosphate(ATP).The specific activity is > 5,000 pmoles/min/ug.
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, 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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