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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
Results find SHIP2 expression negatively regulated by ZIC2 (zeige ZIC2 Antikörper). Its expression is downregulated in osteosarcoma cells and tissues.
The authors report two novel mutations in the INPPL1 gene and show that cell migration is very much decreased in fibroblasts derived from three opsismodysplasia (OPS (zeige LRP5 Antikörper)) patients as compared with control individuals. In contrast, cell adhesion on fibronectin (zeige FN1 Antikörper) is increased in OPS (zeige LRP5 Antikörper) fibroblasts.
Aiming to uncover interdomain regulatory mechanisms in SHIP2, the authors determined crystal structures containing the 5-phosphatase and a proximal region adopting a C2 fold. This reveals an extensive interface between the two domains, which results in significant structural changes in the phosphatase domain.
the expression and intrinsic phosphatase activity of the lipid phosphatase SHIP2 is increased in human colorectal cancer, and that increased expression within a large cohort of CRC (zeige CALR Antikörper) patient is correlated to a worse patient survival. SHIP2 functions as an oncogene (zeige RAB1A Antikörper), by enhancing cell migration and invasion, and reducing cell adhesion in colorectal cancer cells.
HIP2 (zeige UBE2K Antikörper) regulates mitotic spindle alignment. SHIP2 is expressed in G1 phase, whereas Aurora A kinase (zeige AURKA Antikörper) is enriched in mitosis. SHIP2 binds Aurora A kinase (zeige AURKA Antikörper) and the scaffolding protein HEF1 (zeige NEDD9 Antikörper) and promotes their basolateral localization at the expense of their luminal expression connected with cilia resorption.
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.
Inactivation of SHIP2 leads to increased microvilli formation and solute reabsorption by the renal proximal tubule and was associated with hyperactivated ezrin/radixin/moesin (zeige MSN Antikörper) proteins and increased Rho-GTP (zeige AK3 Antikörper).
data suggest that endothelial SHIP2 is required to maintain normal systemic glucose homeostasis and prevent oxidative stress-induced (zeige SQSTM1 Antikörper) endothelial dysfunction.
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.
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