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The protein encoded by LIMS1 is an adaptor protein which contains five LIM domains, or double zinc fingers. Additionally we are shipping LIM and Senescent Cell Antigen-Like Domains 1 Antibodies (69) and LIM and Senescent Cell Antigen-Like Domains 1 Kits (1) and many more products for this protein.
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High LIMS1 expression is associated with Neuroblastoma (show ARHGEF16 Proteins).
focal adhesion signaling to actin cytoskeleton is implicated in human laryngeal carcinogenesis and PINCH1 has prognostic significance in the disease.
that PINCH-1 may be playing an important role in etiopathogenesis of both subtypes breast cancer
Mammalian cells have two functional PINCH proteins, PINCH1 and PINCH2 (show LIMS2 Proteins). PINCH 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).
our data suggest an essential role of PINCH1, ILK (show ILK Proteins) and ILKAP (show ILKAP Proteins) for the radioresistance of p53 (show TP53 Proteins)-wildtype glioblastoma multiforme cells
Data suggest that PINCH1 and Nck2 (show NCK2 Proteins) critically participate in the regulation of cellular radiosensitivity and EGFR (show EGFR Proteins) function and downstream signaling in a cellular model of human squamous cell carcinoma.
Downregulation of PINCH1 is associated with metastatic breast cancer.
changes in CSF (show CSF2 Proteins) levels of PINCH appear to correlate with changes in blood CD4 (show CD4 Proteins) count and with changes in CSF (show CSF2 Proteins) hyperphosphorylated Tau levels
two novel genes, galectin 9 (show LGALS9 Proteins) and PINCH, were expressed at much higher levels in cancerous lesions than in normal tissues in all the patients with clear-cell carcinoma who were examined
PINCH predicts survival in rectal cancer patients with RT, but not in patients without RT. The expression of PINCH may be regulated by radiation and by environmental factors surrounding the cells.
findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK (show ILK Proteins) as well as EPLIN (show LIMA1 Proteins).
Rsu-1 (show RSU1 Proteins) expression is dramatically decreased in PINCH double knockout mouse livers.
PINCH is increased and binds to hp-Tau. These studies address a new mechanism by which AD and HIV may intersect and identify PINCH as a contributing factor to the accumulation of hyperphosphorylated Tau.
PINCH-1 inhibits JNK (show MAPK8 Proteins)-mediated apoptosis by stabilising the PINCH-1 binding protein RSU-1 (show RSU1 Proteins) and promotes Bcl-2 (show BCL2 Proteins)-dependent pro-survival signalling downstream of integrins.
Data suggest that the adapter protein (show GRB10 Proteins) PINCH1 critically participates in the regulation of the cellular radiosensitivity of normal and malignant cells similarly under adhesion and suspension conditions.
PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes.
These results provide important evidence for a crucial role of the PINCH-1-ILK (show ILK Proteins)-alpha-parvin (show PARVA Proteins) complex in the control of podocyte adhesion, morphology, and survival.
LIM (show PDLIM5 Proteins) 5 domain of PINCH1 interacts with Rsu-1 (show RSU1 Proteins) in mammalian cells and functions, in part, by altering cell adhesion.
The PINCH1 is composed of 5 LIM domains, binds ILK and locates to integrin-mediated adhesion sites, and PINCH1 is for integrin function, actin organization, cell-cell adhesion and endodermal cell survival during the implanting of mouse embryos.
PICH1, Ilk (show ILK Proteins) and alpha-parvin (show PARVA Proteins) form a complex to costameres in neonatal mouse ventricular myocytes. This complex is stimulated by fibronectins and phenylephrine, and by both by drug synergism, to regulate cardiac myocyte hypertrophy.
The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading. Several transcript variants encoding different isoforms have been found for this gene.
LIM and senescent cell antigen-like-containing domain protein 1
, particularly interesting new Cys-His protein 1
, renal carcinoma antigen NY-REN-48