The HA tag is derived from an epitope of the influenza hemagglutinin protein, which has been extensively used as a general fusion tag in expression vectors. It has antigenic sites, cleavage sites, receptor binding sites, and fusion peptides mediating membrane fusion.
Inmunógeno
Immunogen Sequence: GI # 1373274, sequence 143-151
Synthetic peptide sequence of HA tag.
Aplicación
Anti-HA tag antibody produced in chicken has been used in immunostaining[1] (1:100).[2]
Acciones bioquímicas o fisiológicas
The hemagglutinin (HA) protein is a key factor of influenza A virus pathogenicity.
Forma física
Solution in phosphate buffered saline containing 0.02% sodium azide.
Cláusula de descargo de responsabilidad
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Current topics in microbiology and immunology, 385, 3-34 (2014-07-18)
The hemagglutinin (HA) is a prime determinant of the pathogenicity of influenza A viruses. It initiates infection by binding to cell surface receptors and by inducing membrane fusion. The fusion capacity of HA depends on cleavage activation by host proteases
Proceedings of the Japan Academy. Series B, Physical and biological sciences, 88(6), 226-249 (2012-06-26)
Influenza virus hemagglutinin (HA) contains antigenic sites recognized by the host immune system, cleavage sites cleaved by host proteases, receptor binding sites attaching to sialyl receptors on the target cell, and fusion peptides mediating membrane fusion. Change in an amino
Ezrin-Radixin-Moesin (ERM) proteins play an essential role in the cytoplasm by cross-linking actin filaments with plasma membrane proteins. Research has identified the nuclear localization of ERMs, as well as the involvement of a single Drosophila ERM protein, Moesin, in nuclear
Biochimica et biophysica acta. Molecular cell research, 1864(10), 1589-1604 (2017-05-31)
Current models imply that the evolutionarily conserved, actin-binding Ezrin-Radixin-Moesin (ERM) proteins perform their activities at the plasma membrane by anchoring membrane proteins to the cortical actin network. Here we show that beside its cytoplasmic functions, the single ERM protein of
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