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Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated

Catalog No. TMPY-06948

Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated is expressed in Baculovirus insect cells with His and Avi tag. The predicted molecular weight is 59.79 kDa and the accession number is AAP34324.1.

Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated

Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated

Catalog No. TMPY-06948
Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated is expressed in Baculovirus insect cells with His and Avi tag. The predicted molecular weight is 59.79 kDa and the accession number is AAP34324.1.
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20 μg$4987-10 days
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Product Information

Biological Activity
Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Influenza A H1N1 (A/New Caledonia/20/1999) Hemagglutinin/HA-specific B cell probe (Y108F, and aa 339-342 SIQS→QRET, His & Avi), Biotinylated is expressed in Baculovirus insect cells with His and Avi tag. The predicted molecular weight is 59.79 kDa and the accession number is AAP34324.1.
Species
H1N1
Expression System
Baculovirus Insect Cells
TagHis, Avi
Accession NumberAAP34324.1
Synonyms
Harvey rat sarcoma viral oncogene homolog
Construction
A DNA sequence encoding the Influenza A virus ((A/New Caledonia/20/1999) (H1N1)) hemagglutinin (translated amino acids of AAP34324.1) (Met1-Val519, Y108F, and aa339-342 SIQS→QRET), termed as HA, was expressed with the bacteriophage T4 fibritin and a polyhistidine tag at the C-terminus. Predicted N terminal: Asp 18
Protein Purity
≥ 95 % as determined by SDS-PAGE.
Molecular Weight59.79 kDa (predicted); 68.2 kDa (reducing conditions)
Endotoxin< 1.0 EU/μg of the protein as determined by the LAL method.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris, 500 mM NaCl, 10% Glycerol, pH 7.5. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage
It is recommended to store recombinant proteins at -20°C to -80°C for future use. 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.
ShippingIn general, Lyophilized powders are shipping with blue ice.
Research Background
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.

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