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PDLIM5 (PDZ and LIM domain 5) Blocking Peptide (100ug)

PDLIM5 (PDZ and LIM domain 5) Blocking Peptide (100ug)

Supplier: Aviva Systems Biology Incorporated
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This is a synthetic peptide designed for use in combination with anti-PDLIM5 antibody (Catalogue #: ARP38796_T100) made by Aviva Systems Biology. It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications. Please inquire for more details.
Presku: AAP38796
Size: 100 ug
Weight: 64kDa
Gene: 10611
Format: Lyophilized powder
Target: PDLIM5 is a LIM domain protein. LIM domains are cysteine-rich double zinc fingers composed of 50 to 60 amino acids that are involved in protein-protein interactions. LIM domain-containing proteins are scaffolds for the formation of multiprotein complexes. The proteins are involved in cytoskeleton organization, cell lineage specification, organ development, and oncogenesis. The encoded protein is also a member of the Enigma class of proteins, a family of proteins that possess a 100-amino acid PDZ domain in the N terminus and 1 to 3 LIM domains in the C terminus. Multiple transcript variants encoding different isoforms have been found for this gene, although not all of them have been fully characterized.The protein encoded by this gene is a LIM domain protein. LIM domains are cysteine-rich double zinc fingers composed of 50 to 60 amino acids that are involved in protein-protein interactions. LIM domain-containing proteins are scaffolds for the formation of multiprotein complexes. The proteins are involved in cytoskeleton organization, cell lineage specification, organ development, and oncogenesis. The encoded protein is also a member of the Enigma class of proteins, a family of proteins that possess a 100-amino acid PDZ domain in the N terminus and 1 to 3 LIM domains in the C terminus. Multiple transcript variants encoding different isoforms have been found for this gene, although not all of them have been fully characterized.
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