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. 2004 Nov 23;384(Pt 2):255–262. doi: 10.1042/BJ20040344

Figure 1. (A) Schematic representation of the predicted functional domains of ROCK I, and (B) SDS/PAGE of purified full-length ROCK I and II and the four truncated ROCK I constructs.

Figure 1

(A) The limits of the four ROCK truncations are shown below the full-length sequence. Both full-length ROCK I (1354 amino acids) and ROCK II (1388 amino acids) and the four ROCK I constructs were cloned and expressed in insect cells. (B) Standard protein markers (lane 1) in the order of increasing molecular mass are: lysozyme (14.4 kDa), soybean trypsin inhibitor (21.5 kDa), carbonic anhydrase (31 kDa), ovalbumin (45 kDa), BSA (66.2 kDa), and phosphorylase b (97.4 kDa). The identities of the sample proteins are: lane 2, full-length ROCK II; lane 3, S6–L553; lane 4, S6–R415; lane 5, S6–E379; lane 6, M71–E379; lane 7, full–length ROCK I.

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