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PDLIM2 encodes a member of the ALP subfamily of PDZ-LIM domain proteins. Additionally we are shipping PDLIM2 Proteins (7) and many more products for this protein.
Showing 10 out of 44 products:
Human Polyclonal PDLIM2 Primary Antibody for WB - ABIN528596
Zhao, Yasunaga, Satou, Nakao, Takahashi, Fujii, Matsuoka: Human T-cell leukemia virus type 1 bZIP factor selectively suppresses the classical pathway of NF-kappaB. in Blood 2009
Deficiency in PDLIM2 resulted in the accumulation of STAT3 (show STAT3 Antibodies) in the nucleus, enhanced the extent of TH17 cell differentiation, and exacerbated granuloma formation.
Pdlim2 is a novel actin-regulating protein of podocyte foot processes that may have a role in the pathogenesis of glomerular diseases.
OPN (show SPP1 Antibodies) was necessary for PDLIM2 serine phosphorylation and STAT1 (show STAT1 Antibodies) ubiquitination in bone marrow macrophages.
PDLIM2 expression was sufficient to suppress in vitro anchorage-independent growth and in vivo tumor formation of colon cancer. PDLIM2 repression involves promoter methylation.
Knockdown of Mystique 2 with small interfering RNA abrogated both adhesion and migration in MCF10A and MCF-7 cells
SLIM is a novel ubiquitin E3 ligase whose targets include STAT (show STAT1 Antibodies) proteins.
PDLIM2 deficiency resulted in larger amounts of nuclear p65 (show NFkBP65 Antibodies), defective p65 (show NFkBP65 Antibodies) ubiquitination and augmented production of proinflammatory cytokines in response to innate stimuli
Stat-interacting LIM protein as the critical Stat (show STAT1 Antibodies) ubiquitin E3 ligase involved in osteopontin (show SPP1 Antibodies) regulation of Stat1 (show STAT1 Antibodies).
Suppression of PDLIM2 expression resulted in decreased cell adhesion, increased NF-kappaB (show NFKB1 Antibodies) transcription reporter activity, and increased LPS (show TLR4 Antibodies)-induced TNF-alpha (show TNF Antibodies) production.
The suppression of PDLIM2 expression significantly reduced cell proliferation, cell growth and neoplasm invasiveness in prostate cancer cells.
epigenetic repression of PDLIM2 can be reversed by 5-aza-2-deoxycytidine and vitamin D to suppress KSHV-associated cancer cell growth
PDLIM2 expression is essential for feedback regulation of the beta1-integrin-RhoA (show RHOA Antibodies) signalling axis and integration of cellular microenvironment signals with gene expression to control the polarity of breast epithelial acini structures.
PDLIM2 integrates cytoskeleton signaling with gene expression in epithelial differentiation by controlling the stability of key transcription factors and COP9 (show COPS8 Antibodies) signalosome activity.
PDLIM2 was a direct target gene of 1,25(OH)2D3
PDLIM2 binds to Tax (show CNTN2 Antibodies) directly, which was mediated by a putative alpa-helix motif of PDLIM2 at amino acids 236-254.
PDLIM2, an essential terminator of NF-kappaB (show NFKB1 Antibodies) activation, is repressed in both estrogen receptor (show ESR1 Antibodies)-positive and estrogen receptor (show ESR1 Antibodies)-negative breast cancer cells, suggesting one important mechanism for the constitutive activation of NF-kappaB (show NFKB1 Antibodies).
Data show that the PDLIM2 repression was independent of the viral regulatory protein Tax (show CNTN2 Antibodies) because neither short-term induction nor long-term stable expression of Tax (show CNTN2 Antibodies) could downregulate PDLIM2 expression.
This gene encodes a member of the ALP subfamily of PDZ-LIM domain proteins. The encoded protein suppresses anchorage-dependent growth and promotes cell migration and adhesion through interactions with the actin cytoskeleton via the PDZ domain. The encoded protein is also a putative tumor suppressor protein, and decreased expression of this gene is associated with several malignancies including breast cancer and adult T-cell leukemia. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
PDZ and LIM domain protein 2
, PDZ-LIM protein mystique
, STAT-interacting LIM protein
, alpha-actinins and filamin-interacting protein