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Product Details
Source
Chimeric Monoclonal Anti-Human parainfluenza viruses Pre-fusion glycoprotein F0 Antibody, Human IgG1 (15A10) is recombinantly expressed in HEK293. It consists of mouse variable regions genetically fused to human IgG1 constant domains.
Antibody Type
Recombinant Monoclonal
Clone
15A10
Isotype
Human IgG1, Kappa
Host Species
Mouse
Reactivity
Virus
Immunogen
Recombinant Human parainfluenza viruses Pre-fusion glycoprotein F0 is expressed from human 293 cells
Specificity
Specifically recognizes Human parainfluenza viruses Pre-fusion glycoprotein F0.
Application
ApplicationRecommended Use / PerformanceWestern Blot10-0.1 μg/mLELISA0.2-2 μg/mLPurification
Protein A purified.
Aggregation
Less than 10%, as determined by SEC-MALS.
Concentration
Please refer to the Certificate of Analysis (CoA).
Form
Lyophilized
Formulation
Lyophilized from a 0.22 μm-filtered solution in PBS (pH 7.4), with trehalose as protectant.
Please contact us for customized product forms or formulations.
Reconstitution
Please refer to the Certificate of Analysis (CoA) for specific instructions.
Shipping
Lyophilized product is shipped at ambient temperature.
Storage
For long term storage, the product should be stored in a lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Notices
Product Specific Notices: For research use only.
ACRO Quality Management System
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Data Display
Bioactivity-ELISA
Immobilized Human parainfluenza viruses Pre-fusion glycoprotein F0, His Tag (Cat. No. PR0-H52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Human parainfluenza viruses Pre-fusion glycoprotein F0 Antibody, Human IgG1 (15A10) (Cat. No. HPV-MY2325) with a linear range of 0.04-2 ng/mL (QC tested).
Protocol
Western Blot
Western blot analysis of Human parainfluenza viruses Pre-fusion glycoprotein F0, His Tag (Cat. No. PR0-H52H3). The protein was loaded at 400 ng per lane and detected using Monoclonal Anti-Pre-fusion glycoprotein F0 (Human parainfluenza viruses) Antibody, Human IgG1 (15A10) at 0.1 μg/mL, followed by HRP-conjugated Goat Anti-Human IgG, Fcγ fragment specific secondary antibody at a 1:2000 dilution. A specific band was detected at approximately 60-70 kDa.
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FAQ
- product
Can lyophilized proteins remain stable during room-temperature shipping or temporary room-temperature exposure?
In general, lyophilized proteins remain stable during room-temperature shipping or temporary exposure to room-temperature conditions.
Many ACROBiosystems recombinant proteins are supplied in lyophilized (freeze-dried) form. The lyophilization process effectively removes moisture from the product, helping reduce degradation-related reactions and improve protein stability during transportation and storage.
To evaluate the stability of lyophilized proteins under normal temperature conditions, ACROBiosystems conducted a stability study on 11 representative lyophilized protein products at 37°C. The study demonstrated that these proteins maintained good quality stability after storage at 37°C for approximately 20 days. Based on these validation results, temporary room-temperature exposure during shipping or handling is generally not expected to have a significant impact on product quality or downstream application performance.
To ensure optimal long-term stability, products should be stored according to the storage conditions specified in the product Certificate of Analysis (COA) upon receipt.
Supporting Document
- Product
What do “pre” and “post” refer to in the names of viral proteins?
In virology, “pre” refers to the conformation of a viral surface glycoprotein before fusion with the host cell membrane, while “post” refers to the conformation after membrane fusion and entry into the host cell. Both are naturally occurring states in the viral life cycle. Because the “pre” conformation represents a critical stage before viral entry, antibodies designed against this state often exhibit stronger neutralizing activity and are therefore more effective in preventing infection.
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