HA-tag Protein Expression, Production, and Purification Basics

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What is an 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 or the biodistribution of the recombinant HA-tagged protein.

What is the HA-tag Peptide's Nucleotide and Amino Acid Sequence?

The HA tag's nucleotide sequence is: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3'

The HA tag's amino acid sequence is: YPYDVPDYA

What is the Molecular Wieght of the HA-tag?

The molecular weight of the HA-tag (YPYDVPDYA-tag) peptide is 1102.15 Da.

Why use an HA-tag for protein expression and production?

Adding an HA-tag to a protein's C- or N-terminus can facilitate its detection, isolation, and purification by HA-tag specific antibodies. Sino Biological has developed HA-tag specific antibodies for ELISA, Western Blotting, Immonofluorecence, and Immunoprecipitation detection of the HA-tagged protein. It can also be conjugated to agarose beads for HA-tagged protein affinity purification.

How to Purify HA-tagged Proteins?

HA-tagged recombinant protein can be affinity purified directly from a cell culture lysate or supernatant. 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 affnity column by high concentration of the HA-tag peptide or by low pH buffer. For more information on usage of the HA-tag affinity purification resin, please refer to: HA-tag Affinity Resin.

How do I cleave of the HA-tag after purification?

In some applications, it is desirable to remove the HA-tag, for example, for protein crystalization. To allow cleavage of the HA-tag, a protease cleavage site needs to be engineered between the tag and the protein. 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. For more information on the cleavage site and tag removal by EK and HRV-3C protease, please refer to: Enterokinase (EK), HRV-3C (human rhinovirus protease).

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