Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human INPPL1 Protein expressed in Wheat germ - ABIN1307967
Zhou, Liu, Tan: Prognostic value of elevated SHIP2 expression in laryngeal squamous cell carcinoma. in Archives of medical research 2012
article focuses on the mutations associated with opsismodysplasia and explores the role of INPPL1/ SHIP2 in skeletal development (Review)
SHIP2 recruits Mena (show EGFR Proteins) to invadopodia and disruption of SHIP2-Mena (show EGFR Proteins) interaction in cancer cells leads to attenuated capacity for ECM (show MMRN1 Proteins) degradation and invasion in vitro, as well as reduced metastasis in vivo.
In glioblastoma 1321 N1 cells, we recently identified Myo1c (show MYO1C Proteins) as a new interactor of SHIP2. SHIP2 localization at lamellipodia and ruffles is impaired in Myo1c (show MYO1C Proteins) depleted cells. In the absence of Myo1c (show MYO1C Proteins), N1 cells tend to associate to form clusters.
decreased expression of transcription factor Sp1 (show SP1 Proteins) 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 (show EPHA2 Proteins)-SHIP2 SAM-SAM (show TTN Proteins) domain heterodimer complex the dissociation process of the EphA2 (show EPHA2 Proteins)-SHIP2 SAM-SAM (show TTN Proteins) domain heterodimer complex
Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt (show AKT1 Proteins).
these findings suggest that SHIP2 is an important regulator of hepatic lipogenesis and lipoprotein secretion in insulin (show INS Proteins) resistance state.
investigated the molecular link between SHIP2 expression and metabolic dyslipidemia using overexpression or suppression of SHIP2 gene in HepG2 cells
These findings suggest that palmitate contributes to SHIP2 overexpression in skeletal muscle via the mechanisms involving the activation of ceramide-JNK (show MAPK8 Proteins) and NF-kappaB (show NFKB1 Proteins) pathways.
results suggest that SHIP2 contributes to the regulation of food intake mainly via the attenuation of insulin (show INS Proteins) 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 (show INS Proteins)/IGF-I (show IGF1 Proteins) actions in the brain, and excess amounts of SHIP2 may be related, at least in part, to brain dysfunction in insulin (show INS Proteins) resistance with type 2 diabetes.
The SHIP2 is a negative regulator of insulin (show INS Proteins) signaling, our findings suggest the importance of the phosphoinositide metabolism at endocytic clathrin-coated pits in the regulation of insulin (show INS Proteins) signal output.
Association with the insulin (show INS Proteins) resistance of diabetic db/db (show LEPR Proteins) mice.
The role of SHIP2 in controlling phosphatidylinositol 3,4,5-trisphosphate levels in platelets.
SH2-containing inositol phosphatase 2 predominantly regulates Akt2 (show AKT2 Proteins), and not Akt1 (show AKT1 Proteins), phosphorylation at the plasma membrane in response to insulin (show INS Proteins) in adipocytes
SHIP2 plays an important role in the negative regulation of insulin (show INS Proteins) signaling for protein synthesis and the impact of SHIP2 is altered, dependent on the acute or chronic exposure of excess concentrations of amino acids in culture.
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