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Figure 1 | Journal of Molecular Signaling

Figure 1

From: Dramatic inhibition of osteoclast sealing ring formation and bone resorption in vitro by a WASP-peptide containing pTyr294 amino acid

Figure 1

A. Schematic diagram demonstrating various WASP constructs generated in HA-TAT expression vector. The domain organization of WASP is shown in full length WASP (WASP-FL). These domains (BR, basic region; GBD, GTPase binding domain; GP, GTPase binding domain and proline rich domain; Pro, proline-rich region; Verpolin-like, central, and acidic domain [VCA]; Verpolin-like, and central domain [VC]) are cloned separately into the HA-TAT expression vector. The number within the parentheses indicates the first and last amino acid of the corresponding WASP peptide. B. SDS-PAGE analysis demonstrates the purified TAT-fused WASP and control (Hsv-TK and HA-TAT) proteins. TAT-fused proteins were subjected to 8% (lanes 1–3) and 15% (lanes 4–9) SDS-PAGE and stained with Coomassie blue. The numbers on the left of each panel represent the standard molecular weight (MW) markers (kDa). The numbers on the top of each lane indicate the apparent molecular mass (kDa) of the purified protein.

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Journal of Molecular Signaling

ISSN: 1750-2187