The LIM domain of PDLIM1 interacts with the C-terminal EF-hand region of alpha-actinin-2 (ACTN2). Immunoprecipitation, Western blot analysis, and immunofluorescence microscopy demonstrated that the 36-kD PDLIM1 protein colocalizes with ACTN2 in the Z discs of myocardial sarcomeres, particularly at intercalated discs, and with vinculin (VCL), which is localized in the fascia adherens of intercalated discs.
Sequence analysis predicted that the 329-amino acid PDLIM1 protein, which is 88% homologous to the rat protein, shares 51 to 61% identity with the PDZ domains of ENIGMA, ALP, ENH, and RIL. SDS-PAGE analysis showed that recombinant PDLIM1 was expressed as a 36-kD protein.
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