Analytical Data
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Gene name
HMPV
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简介
Fusion glycoprotein F0 is cleaved to generate mature F1 and F2 fusion glycoproteins. It transitions through different conformational states to promote the fusion of virus and cell membranes. HMPV Protein, Human (HEK293, His) is the recombinant virus-derived HMPV protein, expressed by HEK293, with C-His labeled tag.
- Application
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Alternative Names
Fusion glycoprotein F0; Protein F
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Species
Virus
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6WB98
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Expression Region
L19-T489
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Protein Length
Partial
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Molecular Weight
70.2 kDa & 50.5 kDa & 17.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Human metapneumovirus (HMPV) is a significant respiratory pathogen, particularly in infants, the elderly, and immunocompromised individuals. First identified in the early 2000s, HMPV is known to cause upper and lower respiratory tract infections, leading to severe clinical outcomes. Due to its genetic diversity and ability to evade the immune response, effective vaccines and treatments remain challenging. Research into HMPV recombinant proteins has gained momentum, as these proteins can serve as potential candidates for vaccine development and diagnostic tools. Recombinant proteins derived from various viral proteins, such as the fusion (F) and attachment (G) proteins, elicit robust immune responses, making them ideal for eliciting both humoral and cellular immunity. Understanding the structure and function of these proteins is crucial for developing effective vaccines that can offer cross-protection against diverse strains. Additionally, studying HMPV recombinant proteins aids in the elucidation of viral pathogenesis and immune evasion mechanisms. Overall, HMPV recombinant protein research is pivotal for addressing the public health concerns posed by this virus, paving the way for effective prevention and therapeutic strategies.
