Name :
Recombinant Human IFN-alpha B2/IFNA8 Protein
Biological Activity :
Background :
Interferon alpha-B, also known as IFNA8, belongs to the alpha/beta interferon family. Interferons are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They also allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. Interferons also activate immune cells, such as natural killer cells and macrophages. They increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes. They also increase the ability of uninfected host cells to resist new infections by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Produced by macrophages, IFN-alpha has antiviral activities.
Biological Activity :
Measured in antiviral assays using WISH cells infected with vesicular stomatitisvirus (VSV). The ED50 for this effect is 0.2-2 pg/mL.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_002161.2
NCBI Gene ID :
Synonyms :
Synonyms :
interferon, alpha 8
Amino Acid Sequence :
Molecular Weight :
The secreted recombinant human IFNA8 consists of 168 amino acids and predicts a molecular mass of 19.6 KDa. The apparent molecular mass of the protein is approximately 26 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity :
> 95 % 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 human IFNA8 (NP_002161.2)(Cys24-Glu189) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
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 :
IFN-alphaB Protein, Human IFN-alpha B2/IFNA8 背景信息 Interferon alpha-B, also known as IFNA8, belongs to the alpha/beta interferon family. Interferons are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They also allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. Interferons also activate immune cells, such as natural killer cells and macrophages. They increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes. They also increase the ability of uninfected host cells to resist new infections by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Produced by macrophages, IFN-alpha has antiviral activities.
References & Citations :
Henco K. et al., 1985, J Mol Biol. 185 (2): 227-60. Goeddel DV. et al., 1981, Nature. 290 (5801): 20-6. Yelverton E. et al., 1981, Nucleic Acids Res. 9 (3): 731-41. Kempaiah P. et al., 2012, Hum Genet. 131 (8): 1375-91.
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