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Human Polyclonal INPPL1 Primary Antibody für ICC, IF - ABIN151139
Yoshinaga, Ohkubo, Sasaki, Nuriya, Ogawa, Yasui, Tabata, Nakajima: A phosphatidylinositol lipids system, lamellipodin, and Ena/VASP regulate dynamic morphology of multipolar migrating cells in the developing cerebral cortex. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2012
article focuses on the mutations associated with opsismodysplasia and explores the role of INPPL1/ SHIP2 in skeletal development (Review)
SHIP2 recruits Mena (zeige EGFR Antikörper) to invadopodia and disruption of SHIP2-Mena (zeige EGFR Antikörper) interaction in cancer cells leads to attenuated capacity for ECM (zeige MMRN1 Antikörper) degradation and invasion in vitro, as well as reduced metastasis in vivo.
In glioblastoma 1321 N1 cells, we recently identified Myo1c (zeige MYO1C Antikörper) as a new interactor of SHIP2. SHIP2 localization at lamellipodia and ruffles is impaired in Myo1c (zeige MYO1C Antikörper) depleted cells. In the absence of Myo1c (zeige MYO1C Antikörper), N1 cells tend to associate to form clusters.
decreased expression of transcription factor Sp1 (zeige SP1 Antikörper) contributes to suppression of SHIP2 in gastric cancer cells.
In order to shed light on the role of the C2 related (C2R) domain, immediately C-terminal to the SHIP2 phosphatase domain, molecular cloning, expression, purification and crystallization of the human SHIP2 fragment containing the phosphatase (Ptase) and C2R domains were performed an X-ray crystallographic data analysis was conducted.
Regulation of phosphatidylinositol 4,5-bisphosphate by SHIP2 controls glioblastoma cell migration through the organization of focal adhesions.
the dissociation process of the EphA2 (zeige EPHA2 Antikörper)-SHIP2 SAM-SAM (zeige TTN Antikörper) domain heterodimer complex the dissociation process of the EphA2 (zeige EPHA2 Antikörper)-SHIP2 SAM-SAM (zeige TTN Antikörper) domain heterodimer complex
Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt (zeige AKT1 Antikörper).
these findings suggest that SHIP2 is an important regulator of hepatic lipogenesis and lipoprotein secretion in insulin (zeige INS Antikörper) resistance state.
investigated the molecular link between SHIP2 expression and metabolic dyslipidemia using overexpression or suppression of SHIP2 gene in HepG2 cells
The authors concluded that the FcgammaRIIb-SHIP2 axis links Abeta (zeige APP Antikörper) neurotoxicity to tau pathology by dysregulating phosphoinositide metabolism, providing insight into therapeutic potential against Alzheimer's disease.
These findings suggest that palmitate contributes to SHIP2 overexpression in skeletal muscle via the mechanisms involving the activation of ceramide-JNK (zeige MAPK8 Antikörper) and NF-kappaB (zeige NFKB1 Antikörper) pathways.
results suggest that SHIP2 contributes to the regulation of food intake mainly via the attenuation of insulin (zeige INS Antikörper) signalling in the hypothalamus of mice
The catalytically-inactive Ship2 mutant protein in a context of reduced PtdIns(4,5)P2 3-kinase activity.
Regulation of insulin signaling and glucose transporter 4 (GLUT4) exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase, skeletal muscle, and kidney enriched inositol polyphosphate phosphatase (SKIP).
These results suggest that SHIP2 is a potent negative regulator of insulin (zeige INS Antikörper)/IGF-I (zeige IGF1 Antikörper) actions in the brain, and excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin (zeige INS Antikörper) resistance with type 2 diabetes.
The SHIP2 is a negative regulator of insulin (zeige INS Antikörper) signaling, our findings suggest the importance of the phosphoinositide metabolism at endocytic clathrin-coated pits in the regulation of insulin (zeige INS Antikörper) signal output.
Association with the insulin (zeige INS Antikörper) resistance of diabetic db/db (zeige LEPR Antikörper) mice.
The role of SHIP2 in controlling phosphatidylinositol 3,4,5-trisphosphate levels in platelets.
SH2-containing inositol phosphatase 2 predominantly regulates Akt2 (zeige AKT2 Antikörper), and not Akt1 (zeige AKT1 Antikörper), phosphorylation at the plasma membrane in response to insulin (zeige INS Antikörper) in adipocytes
we suggest that SHIP2 might play a role in the regulation of skeletal muscle development in pigs
The protein encoded by this gene is an SH2-containing 5'-inositol phosphatase that is involved in the regulation of insulin function. The encoded protein also plays a role in the regulation of epidermal growth factor receptor turnover and actin remodelling. Additionally, this gene supports metastatic growth in breast cancer and is a valuable biomarker for breast cancer.
SH2-domain-containing inositol 5-phosphatase 2b
, inositol polyphosphate phosphatase-like 1
, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2-like
, 51C protein
, SH2 domain-containing inositol 5'-phosphatase 2
, SH2 domain-containing inositol-5'-phosphatase 2
, phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
, phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
, protein 51C
, SH2 domain-containing inositol phosphatase 2
, ablSH3-binding protein
, inositol polyphosphate phosphatase-like protein 1
, SH2-containing inositol phosphatase 2