Recombinant Human respiratory syncytial virus (RSV) Fusion protein / RSV-F (Strain RSS-2) Protein (His Tag)

Name: Recombinant Human respiratory syncytial virus (RSV) Fusion protein / RSV-F (Strain RSS-2) Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4953
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	P11209
Description	The extracellular domain of human RSV (strain RSS-2) fusion protein (P11209) (Met 1-Thr 529) was produced with a His tag at the C-terminus.
Source	Insect Cells
Predicted N Terminal	Phe 22
AA Sequence	Met 1-Thr 529
Molecular Weight	The secreted recombinant human RSV (strain RSS-2) comprises 519 amino acids with a predicted molecular mass of 57.8 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 63 kDa and 44-53 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 20mM Tris, 500mM NaCl, pH 7.4, 10% gly
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.

Target Details

Target Function	Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.; Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein may trigger p53-dependent apoptosis.; Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein seems to trigger p53-dependent apoptosis.
Subcellular Location	[Fusion glycoprotein F0]: Host Golgi apparatus membrane; Single-pass membrane protein.; [Fusion glycoprotein F1]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.; [Fusion glycoprotein F2]: Virion membrane. Host cell membrane.
Protein Families	Paramyxoviruses fusion glycoprotein family

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.