推荐产品
生物来源
chicken
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
buffered aqueous solution
制造商/商品名称
Genway 15-288-22511
技术
indirect ELISA: suitable
运输
wet ice
储存温度
−20°C
靶向翻译后修饰
unmodified
一般描述
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.
应用
Anti-HA tag antibody produced in chicken has been used in immunostaining (1:100).
生化/生理作用
The hemagglutinin (HA) protein is a key factor of influenza A virus pathogenicity.
外形
Solution in phosphate buffered saline containing 0.02% sodium azide.
免责声明
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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储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
Eva Böttcher-Friebertshäuser et al.
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
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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