Difference between revisions of "Part:BBa K2872003"
| Line 1: | Line 1: | ||
| + | |||
| + | |||
| + | ===Biology and Usage=== | ||
| + | |||
| + | This part codes for 3x 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] | ||
| + | <br> | ||
| + | |||
| + | '''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. | ||
| + | <br> | ||
| + | [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. | ||
Revision as of 11:31, 17 October 2018
Biology and Usage
This part codes for 3x 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.