Recombinant Human IFNα2 Protein(Trx Tag)

  • 货号:GPEH1119
Recombinant Human IFNα2 Protein(Trx Tag)
  • Recombinant Human IFNα2 Protein(Trx Tag)

Price: ¥10400.00 ¥3600.00 ¥1200.00 ¥16000.00

Size:
500 μg 100 μg 20 μg 1 mg
别称
Interferon alpha-2;LeIF D;Leukocyte interferon
表达系统
E.coli
序列
Cys24-Glu188
蛋白编码
P01563
种属
Human
计算分子量
38.0 kDa
表观分子量
35 kDa
标签
N-Trx
生物活性
Not validated for activity
纯度
> 95% as determined by reducing SDS-PAGE.
内毒素
< 10 EU/mg of the protein as determined by the LAL method
保存条件
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
运输条件
This product is provided as lyophilized powder which is shipped with ice packs.
制剂
Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
复溶方法
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis
背景
Interferon-alpha 2 (IFN alpha-2) is one of 14 subtypes with anin the IFN-alpha class of Type I Interferons. The members of the IFN-alpha class, also known as alpha leukocyte interferons, encompass a group of distinct but closely related proteins which share approximately 80% amino acid (aa) sequence identity and have a similar globular structure composed of five alpha-helices. IFN-alpha class members signal through a common cell surface receptor complex composed of IFN-alpha R2 and IFN-alpha R1 subunits. As the first highly active IFN to be cloned and produced, IFN alpha-2 has become the prototypic IFN for academic and pharmaceutical research. The mature extracellular domain (ECD) of mouse IFN alpha-2 shares 60% and 83% aa sequence identity with an human and rat, respectively. Murine IFN-alpha 2 can eliminate cardiac viral load and protect cardiomyocytes from injury in animals infected with an coxsackievirus B3 (CVB3). IFN alpha-2 derived mutants with an reduced IFNR2 binding inhibited HIV replication and mutants with an more IFNAR1 binding potentiated antiviral activity.
SDS-PAGE analysis of Human IFNα2 proteins, 2μg/lane of Recombinant Human IFNα2 proteins was resolved with SDS-PAGE under reducing conditions, showing bands at 35 kDa
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