GW22511
Anti-HA tag antibody produced in chicken
affinity isolated antibody
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About This Item
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biological source
chicken
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
manufacturer/tradename
Genway 15-288-22511
technique(s)
indirect ELISA: suitable
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
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.
Application
Anti-HA tag antibody produced in chicken has been used in immunostaining (1:100).
Biochem/physiol Actions
The hemagglutinin (HA) protein is a key factor of influenza A virus pathogenicity.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide.
Disclaimer
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Nongluk Sriwilaijaroen et al.
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
Csaba Bajusz et al.
The FEBS journal, 288(16), 4812-4832 (2021-02-20)
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
Ildikó Kristó et al.
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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