Human metapneumovirus (strain CAN97-83) Fusion glycoprotein F0 (His & SUMO)

Catalog No. TMPH-01671

Inactive precursor that is cleaved 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.; 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.

Human metapneumovirus (strain CAN97-83) Fusion glycoprotein F0 (His & SUMO)

Catalog No. TMPH-01671

Pack Size	Price	Availability
20 μg	$360	20 days
100 μg	$678	20 days
1 mg	$2,300	20 days

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Product Information

Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	Inactive precursor that is cleaved 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.; 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.
Species	HMPV
Expression System	E. coli
Tag	N-6xHis-SUMO
Accession Number	Q6WB98
Synonyms	Fusion glycoprotein F0,F
Amino Acid	KESYLEESCSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSR
Construction	20-102 aa
Protein Purity	> 90% as determined by SDS-PAGE.
Molecular Weight	22.3 kDa (predicted)
Formulation	If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Reconstitute the lyophilized protein in sterile deionized water. The product concentration should not be less than 100 μg/mL. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background	Inactive precursor that is cleaved 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.; 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.

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