Recombinant Human respiratory syncytial virus (RSV) (A2) Fusion glycoprotein / RSV-F Protein (His Tag)

Name: Recombinant Human respiratory syncytial virus (RSV) (A2) Fusion glycoprotein / RSV-F Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4952
Availability: InStock

Collections: Featured viral antigens molecules, Other viral antigens, Recombinant proteins, Viral antigen

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Product Overview

Tag	His
Host Species	Human respiratory syncytial virus
Accession	P03420.1
Background	Human orthopneumovirus- (also known as- human respiratory syncytial virus, or- HRSV) is a- syncytial- virus- that causes- respiratory tract- infections. It is a major cause of- lower respiratory tract infections- and hospital visits during infancy and childhood.- Human respiratory syncytial virus is a medium-sized (120-200- nm) enveloped virus that contains a linear negative-sense RNA genome (must be converted to a positive RNA prior to translation). The former contains virally encoded F, G, and SH- lipoproteins. The F and G lipoproteins are the only two that target the cell membrane, and are highly conserved among RSV isolates. HRSV is divided into two antigenic subgroups, A and B, on the basis of the reactivity of the virus with monoclonal antibodies against the attachment (G) and fusion (F).
Description	The extracellular domain of human RSV Fusion glycoprotein (P03420.1) (Met 1-Thr 529) was produced in Baculovirus-Insect Cells and fused with a His tag at the C-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Phe 22
AA Sequence	Met 1-Thr 529
Molecular Weight	The secreted recombinant human RSV-F comprises 518 amino acids with a predicted molecular mass of 58 kDa. The RSV F0 precursor protein is cleaved into the disulfide-linked F1 and F2 subunits. As a result of glycosylation, the apparent molecular mass of the protein is approximately 45-55 kDa and 18 kDa in SDS-PAGE under reducing conditions, corresponding to the two subunits respectively.
Purity	Greater than 95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	This product was lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 10% glycerol
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

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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.