Tag

Part:BBa_K2872003:Design

Designed by: Dina Altarawneh   Group: iGEM18_CMUQ   (2018-10-10)
Revision as of 11:18, 10 October 2018 by Dtarawne (Talk | contribs)


Human influenza hemagglutinin (HA) tag


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 641
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 628


Part information

This part codes for human influenza hemagglutinin (HA) molecule and is fused with a stop codon (taa) at the C-terminus.

HA tag: An HA-tag is derived from the human influenza hemagglutinin (HA) molecule corresponding to amino acids 98-106. It has been extensively used as a general epitope tag in expression vectors. The HA-tag does not appear to interfere with the bioactivity of the recombinant HA-tagged protein. [1]

Purification: The HA-tagged protein binds to the HA-tag specific monoclonal antibody conjugated on an agarose gel. After washing away residual impurities, bound HA-tag proteins can be eluted off the affinity column by high concentration of the HA-tag peptide or by low pH buffer. An EK cleavage site behind the HA-tag (HA-EK site-protein structure) can allow complete removal of the HA-tag and the cleavage site, leaving no additional amino acids after the specific cleavage of the HA-tag. [2]

Source

Human influenza hemagglutinin is found on the surface of influenza viruses.

References

[1] “Anti-HA Tag.” Razor Tie Artery Foundation Announce New Joint Venture Recordings | Razor & Tie, Rovi Corporation, web.archive.org/web/20100914142422/http://www.millipore.com/catalogue/item/05-904. [2] Schembri, Laura, et al. “The HA Tag Is Cleaved and Loses Immunoreactivity during Apoptosis.” Nature Methods, vol. 4, no. 2, 2007, pp. 107–108., doi:10.1038/nmeth0207-107.