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The protein encoded by PDLIM7 is representative of a family of proteins composed of conserved PDZ and LIM domains. Additionally we are shipping PDLIM7 Antibodies (70) and PDLIM7 Kits (13) and many more products for this protein.
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PDLIM7 is a bona fide skeletal muscle substrate of Nedd4-1 (show NEDD4 Proteins).
findings describe a positive regulatory effect of LMP-1 on BMP-2 (show BMP2 Proteins) expression and BMP-2 (show BMP2 Proteins)-mediated osteogenesis. This effect occurs through activation of ERK1/2 pathway and subsequent upregulation of Runx2 (show RUNX2 Proteins) transactivity.
LMP is an important determinant of weight and length, female bone density, and marrow stromal cell propensity for mineralization.
These findings reveal a novel and unexpected function for Pdlim7 in maintaining proper hemostasis in neonatal and adult mice.
LMP-1 showed spatiotemporal expression patterns during molar development.[LMP-1]
the LIM domain protein Enigma direct (show MDM2 Proteins)ly interacts (show TP53 Proteins) with MDM2 to form a ternary complex with p53 in embryonic fibroblasts
Molecular basis of the overactive osteogenic process may at least in part involve a deregulation of the LMP-related pathway in calvarial cells.
The results showed that LMP-1 inhibited cell apoptosis and induced survivin (show BIRC5 Proteins) expression in nasal natural killer/T-cell lymphoma
The results suggest local transduction with LMP-1 gene promotes osteogenesis and mineralization in distraction osteogenesis.
LMP-1 mRNA level was regulated in a dose-dependent manner after transfection
These results are consistent with a model in which binding of OspE to PDLIM7 during infection regulates the activity of PKC (show PRRT2 Proteins) isoforms that bind to the PDLIM7 LIM (show PDLIM5 Proteins) domain.
LMP1 expression suppressed the expression of Runx2 (show RUNX2 Proteins) and BMP-2 (show BMP2 Proteins) in OS cells.
High Enigma (show PDLIM1 Proteins) expression is associated with breast neoplasms.
A direct interaction of Jab1 (show COPS5 Proteins) with LMP-1, is reported.
Gene transfer of LMP3 upregulated Alkaline Phosphatase, Bone Sialoprotein (show CRISP1 Proteins) and BMP2 (show BMP2 Proteins) gene expression and increased in vitro matrix mineralization in human PDL cell line.
LMP3 induced the successful osteogenic differentiation of AFSC by inducing the expression of osteogenic markers and osteospecific transcription factors.
The protein encoded by this gene is representative of a family of proteins composed of conserved PDZ and LIM domains. LIM domains are proposed to function in protein-protein recognition in a variety of contexts including gene transcription and development and in cytoskeletal interaction. The LIM domains of this protein bind to protein kinases, whereas the PDZ domain binds to actin filaments. The gene product is involved in the assembly of an actin filament-associated complex essential for transmission of ret/ptc2 mitogenic signaling. The biological function is likely to be that of an adapter, with the PDZ domain localizing the LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Alternative splicing of this gene results in multiple transcript variants.
LIM mineralization protein
, PDZ and LIM domain protein 7
, protein enigma
, LIM mineralization protein 2
, enigma (LIM domain protein)
, LIM domain protein
, Lim mineralization protein 3
, enigma protein
, LIM mineralizing protein