Name :
Influenza A H9N2 (A/Guinea fowl/Hong Kong/WF10/99) Hemagglutinin / HA Protein (His Tag)

Biological Activity :

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.

Biological Activity :
Testing in progress

Expression Host :

Source :
HEK293 Cells

Tag :

Protein Accession No. :

NCBI Gene ID :

Synonyms :

Synonyms :
Harvey rat sarcoma viral oncogene homolog

Amino Acid Sequence :

Molecular Weight :
The secreted recombinant influenza A H9N2 HA (A/Guinea fowl/Hong Kong/WF10/99 (H9N2)) comprises 516 amino acids and has a predicted molecular mass of 58.2 kDa. As a result of glycosylation, it migrates as an approximately 65-75 kDa band in SDS-PAGE under reducing conditions.

Purity :
> 97 % as determined by SDS-PAGE

State of Matter :

Product Concentration :

Storage and Stability :
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.

Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method

Protein Construction :
A DNA sequence encoding the extracellular domain (Met 1-Lys 523) of the influenza A H9N2 Hemagglutinin (A/Guinea fowl/Hong Kong/WF10/99 (H9N2)) (AAO46082.1) (HA1+HA2, uncleaved) was expressed, fused with a C-terminal polyhistidine tag.

Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :

References & Citations :
White JM, Hoffman LR, Arevalo JH, et al. Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin. In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.1997Suzuki Y.Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol. Pharm. Bull. 2005. Senne DA, Panigrahy B, Kawaoka Y, et al. Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential. Avian Dis. 1996Donald J. Benton,Influenza hemagglutinin membrane anchor,PNAS,2018

MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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