Interferon alpha 10/IFNA10 Protein, Human, Recombinant (Fc Tag)

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Interferon alpha 10/IFNA10 Protein, Human, Recombinant (Fc Tag): Product Information

Purity
> 85 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured in antiviral assays using WISH human amnion cells infected with vesicular stomatitisvirus (VSV).
The ED50 for this effect is 20-80 pg/mL.
Protein Construction
A DNA sequence encoding the human IFNA10 (P01566) (Cys 24-Asp 189) was fused with the Fc region of human IgG1 at the N-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Glu
Molecule Mass
The recombinant human IFNA10/Fc chimera is a disulfide-linked homodimer. The reduced monomer comprises 427 amino acids with a predicted molecular mass of 48 kDa. AsrhIFNA10/Fc monomer migrates as an approximately 50 kDa band in SDS-PAGE under reducing conditions.
Formulation
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 hard copy of CoA.
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.
Stability & Storage
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.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Interferon alpha 10/IFNA10 Protein, Human, Recombinant (Fc Tag): Images

Measured in antiviral assays using WISH human amnion cells infected with vesicular stomatitisvirus (VSV). The ED50 for this effect is 20-80 pg/mL.

Interferon alpha 10/IFNA10 Protein, Human, Recombinant (Fc Tag): Alternative Names

IFN-alphaC Protein, Human; MGC119878 Protein, Human; MGC119879 Protein, Human

Interferon alpha 10/IFNA10 Background Information

Interferon alpha-1 (IFNA1) is a member of the interferon family. Interferons belong to the group of the regulatory glycoproteins, of low molecular mass. They are the products of infected cell-genome, but not virus, as a consequence of the cause answer by different inductors. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs have other functions: they 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; and they increase the ability of uninfected host cells to resist new infection by virus. Certain host symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Human IFN are divided on the sequence of amino-acids into three groups: Alpha, Beta and Gamma interferons.
Full Name
interferon, alpha 10
References
  • De Veer MJ, et al. (2001) Functional classification of interferon-stimulated genes identified using microarrays. J Leukoc Biol. 69 (6): 912-20.
  • Liu YJ. (2005) IPC: professional type 1 interferon-producing cells and plasmacytoid dendritic cell precursors. Annu Rev Immunol. 23: 275-306.
  • Fensterl V, et al. (2009) Interferons and viral infections. Biofactors. 35 (1): 14-20.
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    IFNA10 related areas, pathways, and other information

  • Exome sequencing identifies novel compound heterozygous IFNA4 and IFNA10 mutations as a cause of impaired function in Crohn's disease patients
    Author
    Xiao, CX;Xiao, JJ;Xu, HZ;Wang, HH;Chen, X;Liu, YS;Li, P;Shi, Y;Nie, YZ;Li, S;Wu, KC;Liu, ZJ;Ren, JL;Guleng, B;
    Year
    2015
    Journal
    Sci Rep
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