Intracisternal A particle promoted polypeptide (IPP) is a member of the kelch family of proteins, characterized by a 50 amino acid repeat which interacts with actin. The kelch domain of IPP consists of six C terminal tandem arranged repeats. IPP may play a role in organizing the actin cytoskeleton.
IPP also contains an N terminal POZ protein protein interaction domain. The POZ domain (also called BTB domain) is present near the N terminus of a fraction of zinc finger proteins and in proteins that contain the pfam01344 motif such as kelch and pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co repressor complexes including N-coR and SMRT.
SDS-PAGE - IPP protein (ab51209)
14% SDS-PAGE gel loaded with ab51209, recombinant human IPP protein (POZ domain).
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