Recombinant Influenza A H3N2 (A/Hong Kong/4801/2014) Neuraminidase / NA (His Tag)

Name: Recombinant Influenza A H3N2 (A/Hong Kong/4801/2014) Neuraminidase / NA (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-5140
Availability: InStock

Collections: Featured viral antigens molecules, Influenza a/b antigen, Recombinant proteins, Viral antigen

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Influenza A H3N2
Description	The Influenza A virus (A/Hong Kong/4801/2014 (H3N2)) neuraminidase (translated amino acids of EPI675797) (His36-Ile469) was produced with a His tag at the N-terminus.
Source	HEK293
Predicted N Terminal	His
AA Sequence	His36-Ile469
Molecular Weight	The recombinant Influenza A virus (A/Hong Kong/4801/2014 (H3N2)) NA consists of 453 amino acids and predicts a molecular mass of 50.5 kDa.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Formulation	This product was lyophilized from sterile PBS, pH 7.4.
Stability	Recombinant antigens are stable for up to 1 year from date of receipt at -80°C
Applications	ELISA; immunogen; WB, etc.
Usage	For Research Use Only
Storage	Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Please avoid repeated freeze-thaw cycles.

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.