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. 2000 Nov 6;1:1. doi: 10.1186/1471-2172-1-1

Figure 1.

Figure 1

Expression and purification of recombinant HA-NFATp in insect cells. (A) Schematic of the functional domains of NFATp. The DNA binding domain is central to the protein and the minimal DNA binding domain is located between amino acids 391 and 583. The N-terminal region (amino acids 1-390) contains an activation domain rich in acidic amino acids and the region of the protein that binds calcineurin and is involved in regulated nuclear localization. The C-terminal region (amino acids 688-921) is unique to NFATp and contains an activation domain that is rich in glutamines. (B) HA-NFATp was purified by anti-HA affinity chromatography from baculovirus-infected Hi-five cell extracts. Portions of insect cell extract containing over-expressed HA-NFATp (lane 1), depleted extract (lane 2), and the purified/eluted HA-NFATp (lane 3) were resolved by SDS-PAGE and stained with coomassie brilliant blue. The position of full-length HA-NFATp is indicated with an arrow. (C) HA-NFATp was purified by DNA affinity chromatography from baculovirus-infected Hi-five cell extracts. Portions of insect cell extract containing over-expressed HA-NFATp (lane 1), depleted extract (lane 2), and the purified/eluted HA-NFATp (lane 3) were resolved by SDS-PAGE and stained with coomassie brilliant blue. The position of full-length HA-NFATp is indicated with an arrow.