Recombinant Measles Virus Fusion Glycoprotein F0 (F) Protein (His)

Name: Recombinant Measles Virus Fusion Glycoprotein F0 (F) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06675P
Price: 680.8 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Measles Virus Fusion Glycoprotein F0 (F) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P69353
Target Symbol	F
Species	Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	QIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTS
Expression Range	24-494aa
Protein Length	Partial
Mol. Weight	55.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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 heptad repeat (HR) 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
Subcellular Location	Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.
Protein Families	Paramyxoviruses fusion glycoprotein family
Database References	KEGG: vg:1489800

Gene Functions References

Cell-to-Cell Measles Virus Spread between Human Neurons Is Dependent on Hemagglutinin and Hyperfusogenic Fusion Protein. PMID: 29298883
L454W F mutant is activated independently of H or the cell receptor that enabled the efficient spread in the central nervous system. PMID: 25670774
Acquisition of enhanced fusion activity through substitutions in the extracellular domain of the F protein may be crucial for measles virus to the extensive spread in the central nervous system and development of subacute sclerosing panencephalitis. PMID: 25520515
Complementation of F mutants with a monomeric, fusion-inactive F variant enriched the F oligomers for heterotrimers containing a single disulfide bond, without affecting fusion complementation profiles compared with standard F protein. PMID: 25157143
F maturation prepares for complex separation after triggering, and the H head domains in prereceptor-bound conformation prevent premature stalk rearrangements and F activation. PMID: 25392208
Thermodynamically stabilized by the N465H substitution, the F protein required elevated temperature as high as 40 degrees C to promote cell-cell fusion, whereas all five DIII mutations caused destabilization of the F protein PMID: 25479085
Authors demonstrate that the measles virus H stalk represents the effector domain for measles virus F triggering. PMID: 23966411
Taken together, these findings reveal that the morbillivirus H protein must lower the activation energy barrier of metastable prefusion F for fusion triggering. PMID: 23077316
The F genes of measles virus isolated in china had no significant genetic variation. PMID: 20084883
The F genes of measles virus in China during 1999-2003 had no sig-nificant changes. PMID: 20077667
residues located in the head domain of the F trimer and the HR-B region contribute jointly to controlling F conformational stability PMID: 16415028
findings show that both M (a fraction of which is modified by ubiquitination) & F proteins individually promote formation of virus-like particles, but they do not act in synergy; we propose that M & F act separately in particle morphogenesis and release PMID: 17374768
These findings suggest a common molecular mechanism and a key role of the F protein for syncytium formation in cells expressing an unidentified third receptor for MV. PMID: 17825451
Tyrosine-based targeting motifs in the H and F glycoproteins play a crucial role for MV replication and spread within lymphocytes, the main target cells of acute MV infection. PMID: 18272759
The partitioning of F, CD46 and CD55 molecules in different membrane microdomains could account for the ability of F to escape complement regulation by the CD55 and CD46 regulators. PMID: 18455798
Alanine-scanning mutagenesis revealed that an F protein with a single mutation of a central TM region leucine (L507A) was more fusogenic than the unmodified F protein while retaining similar kinetics of proteolytic processing. PMID: 18786999
The H-protein and the F-protein mediates the virus cell entry. PMID: 19198562
findings argue against specific protein-protein contacts between the H head & F head domains; support a docking model characterized by short-range contacts between prefusion F head & attachment protein stalk, possibly involving H residues 111, 114 & 118 PMID: 19656895

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.