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Human PTPN11 Protein expressed in Wheat germ - ABIN1316822
Jo, Park, Lee, Ahn, Kim, Park, Choi: SHP-2 binds to caveolin-1 and regulates Src activity via competitive inhibition of CSK in response to H2O2 in astrocytes. in PLoS ONE 2014
High PTPN11 expression is associated with suppression of T lymphocyte function in Melanoma.
PTPN11 mutations are the most common cause of the Noonan syndrome, along with frequent neuroepithelial brain tumors. (Review)
A novel PTPN11 mutation defined in two separate fetuses with Cystic hygroma and associated with Noonan syndrome phenotype is being reported.
High PTPN11 expression is associated with Pancreatic cancer.
SHP-2 acts together with PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) to regulate a ZEB1-miR (show MLXIP Proteins)-200 feedback loop in PDGFRalpha-driven gliomas.
Results provide evidence that repression of SHP-1 (show PTPN6 Proteins), SHP-2 and SOCS-1 (show SOCS1 Proteins) gene expression in patient plasma cells supports the constitutive activation of the JAK (show JAK3 Proteins)/STAT3 (show STAT3 Proteins) pathway and probably leads to higher degrees of bone marrow invasion.
The data presented in the current study reveal that intestinal serotonin transporter (SERT (show SLC6A4 Proteins)) is a target of the tyrosine phosphatase SHP2 and show a novel mechanism by which a common diarrheagenic pathogen, EPEC, activates cellular SHP2 to inhibit SERT (show SLC6A4 Proteins) function.
The effects of SHP2 overexpression and inhibition on fibroblast response to profibrotic stimuli were analyzed in in primary human fibroblasts. SHP2 was down-regulated and lung fibroblasts obtained from patients with IPF, revealing SHP2 was absent within fibroblastic foci sufficient to induce fibroblast-to-myofibroblast differentiation in primary human lung fibroblasts, resulting in reduced cell survival.
PTPN11 variant was identified in a case with a lethal presentation of Noonan syndrome.
our results provide strong evidence that CD244 (show CD244 Proteins) co-operates with c-Kit to regulate leukemogenesis through SHP-2/p27 (show PAK2 Proteins) signaling.
SHP2 supports basal pulmonary endothelial barrier function by coordinating the tyrosine phosphorylation profile of VE-cadherin (show CDH5 Proteins), beta-catenin (show CTNNB1 Proteins), and p190RhoGAP (show GRLF1 Proteins) and the activity of RhoA (show RHOA Proteins).
Inactivation of ALX4/Alx4 (show ALX4 Proteins) causes lacrimal gland aplasia in both human and mouse. These results reveal a key role of Alx4 (show ALX4 Proteins) in mediating FGF-Shp2-FGF signaling in the neural crest for lacrimal gland development.
findings define a novel physiological function of Shp2 in TGF-beta1 (show TGFB1 Proteins)/MMP12 (show MMP12 Proteins)-dependent emphysema, adding insights into potential etiologies for this chronic lung disorder.
Ptpn11 gain-of-function mutations are associated with myeloproliferative neoplasm.
aberrant SHP2 signaling during cardiac development leads to congenital heart disease and adult-onset heart hypertrophy
Data suggest that phosphorylation of Shp2/Ptpn11 at Tyr542 and its translocation to postsynaptic compartment are integral processes in synaptic scaling/homeostasis; Shp2 phosphatase activity is critical to regulation of Ser (show SIGLEC1 Proteins)(P)845 GluA1 (show GRIA1 Proteins) and surface expression of GluA1 (show GRIA1 Proteins) during synaptic scaling. (Shp2/Ptpn11 = protein tyrosine phosphatase non-receptor type 11; GluA1 (show GRIA1 Proteins) = glutamate receptor ionotropic Ampa1 (show GRIA1 Proteins) [alpha 1])
data suggested that deletion of Shp2 impaired IL-25 (show IL25 Proteins) production in bronchial epithelial cells in vitro, but might yet have minor influence on OVA-induced allergic reaction in vivo
The effects of SHP2 overexpression and inhibition on fibroblast response to profibrotic stimuli were analyzed in in the bleomycin model of lung fibrosis by SHP2-lentiviral administration in transgenic mice carrying a constitutively active SHP2 mutation. Mice carrying the Noonan syndrome-associated SHP2 mutation were resistant bleomycin induced pulmonary fibrosis.
Data show aberrant neuronal activity-induced signaling and regulation of gene expression in protein tyrosine phosphatase (show ACP1 Proteins), non-receptor type 11 (Ptpn11D61Y) mutation and suggest that these deficits contribute to the pathophysiology of cognitive impairments in Noonan syndrome (NS).
This study indicates that Shp2 is required to orchestrate macrophage function and regulate host innate immunity against pulmonary bacterial infection.
In conclusion, our data suggest that SIRPalpha signaling through SHP-2-PI3K-Akt2 (show AKT2 Proteins) strongly influences osteoblast differentiation from bone marrow stromal cells.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia. Two transcript variants encoding different isoforms have been found for this gene.
, protein-tyrosine phosphatase 1D
, protein-tyrosine phosphatase 2C
, tyrosine-protein phosphatase non-receptor type 11
, SH2 domain-containing protein tyrosine phosphatase-2
, protein-tyrosine phosphatase SYP
, SH-PTP2 protein tyrosine phosphatase non-receptor type 11
, SH-PTP2 protein tyrosine phosphatase, non-receptor type 11
, encodes catalytic domain
, protein tyrosine phosphatase SH-PTP2
, protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)
, non-receptor type protein tyrosine phosphatase SHP2