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Let-7g controls the motility of mouse myoblasts in cell culture by post-transcriptionally regulating the expression of Pinch-2.
Rsu-1 (show RSU1 Proteins) expression is dramatically decreased in PINCH (show LIMS1 Proteins) double knockout mouse livers.
LIM1 (show LHX1 Proteins) domain only of either PINCH1 (show LIMS1 Proteins) or PINCH2 can prevent ILK (show ILK Proteins) degradation despite their failure to localize to focal adhesions.
Absence of either PINCH1 (show LIMS1 Proteins) or PINCH2 in myocardium leads to exacerbated cardiac injury and deterioration in cardiac function after myocardial infarction.
Mammalian cells have two functional PINCH (show LIMS1 Proteins) proteins, PINCH1 (show LIMS1 Proteins) and PINCH2. PINCH (show LIMS1 Proteins) not only binds to Nck2 (show NCK2 Proteins) and engages in the signaling of growth factor receptors, but also forms a ternary complex with ILK (show ILK Proteins) and parvin (show PARVA Proteins) (IPP (show IPP Proteins) complex).
Data indicate compound heterozygous missense mutations that are predicted to be pathogenic in LIM and senescent cell antigen-like domains 2 protein (LIMS2).
Results defined the functional role of copy number variations involving PINCH-2 in cancer progression based on the field cancerization effect; cell migration and invasion through autocrine and paracrine function as part of the field cancerization effect.
PINCH-2 mRNA is overexpressed in malignant mesothelioma
These results identify a novel nuclear and focal adhesion protein that associates with ILK (show ILK Proteins) and reveals an important role of PINCH-2 in the regulation of the PINCH-1 (show LIMS1 Proteins)-ILK (show ILK Proteins) interaction, cell shape change, and migration.
LIMS2 may be useful as a molecular biomarker and a therapeutic target by increasing its expression and activity in gastric cancer
This gene encodes a member of a small family of focal adhesion proteins which interacts with ILK (integrin-linked kinase), a protein which effects protein-protein interactions with the extraceullar matrix. The encoded protein has five LIM domains, each domain forming two zinc fingers, which permit interactions which regulate cell shape and migration. A pseudogene of this gene is located on chromosome 4. Multiple transcript variants encoding different isoforms have been found for this gene.
LIM and senescent cell antigen-like-containing domain protein 2
, particularly interesting new Cys-His protein 2
, ILK-binding protein
, LIM-like protein 2
, LIM and senescent cell antigen-like domains 1