Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus.
Widely expressed, with highest levels in heart, brain, and skeletal muscle.
Involvement in disease
Defects in PTPN11 are the cause of LEOPARD syndrome type 1 (LEOPARD1) [MIM:151100]. It is an autosomal dominant disorder allelic with Noonan syndrome. The acronym LEOPARD stands for lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and deafness. Defects in PTPN11 are the cause of Noonan syndrome type 1 (NS1) [MIM:163950]. Noonan syndrome (NS) is a disorder characterized by dysmorphic facial features, short stature, hypertelorism, cardiac anomalies, deafness, motor delay, and a bleeding diathesis. Some patients with Noonan syndrome type 1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villomoduolar synovitis (PVNS) when occurring in the jaw or joints. Note=Mutations in PTPN11 account for more than 50% of the cases. Rarely, NS is associated with juvenile myelomonocytic leukemia (JMML). NS1 inheritance is autosomal dominant. Defects in PTPN11 are a cause of juvenile myelomonocytic leukemia (JMML) [MIM:607785]. JMML is a pediatric myelodysplastic syndrome that constitutes approximately 30% of childhood cases of myelodysplastic syndrome (MDS) and 2% of leukemia. It is characterized by leukocytosis with tissue infiltration and in vitro hypersensitivity of myeloid progenitors to granulocyte-macrophage colony stimulating factor. Defects in PTPN11 are a cause of metachondromatosis (MC) [MIM:156250]. It is a skeletal disorder with radiologic fetarures of both multiple exostoses and Ollier disease, characterized by the presence of multiple enchondromas and osteochondroma-like lesions.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily. Contains 2 SH2 domains. Contains 1 tyrosine-protein phosphatase domain.
The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.
Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins.
Protein tyrosine phosphatase non receptor type 11 antibody
Protein-tyrosine phosphatase 1D antibody
Protein-tyrosine phosphatase 2C antibody
SH2 domain containing protein tyrosine phosphatase 2 antibody
SHP 2 antibody
Tyrosine-protein phosphatase non-receptor type 11 antibody
Anti-SHP2 antibody images
Western blot - Anti-SHP2 antibody (ab80611)
All lanes : Anti-SHP2 antibody (ab80611) at 0.1 µg/ml
Lane 1 : Whole
cell lysate from HeLa cells at 50 µg Lane 2 : Whole
cell lysate from HeLa cells at 15 µg Lane 3 : Whole
cell lysate from HeLa cells at 5 µg Lane 4 : Whole
cell lysate from 293T cells at 50 µg Lane 5 : Whole
cell lysate from mouse NIH3T3 cells at 50 µg
Developed using the ECL technique
Predicted band size : 68 kDa Observed band size : 68 kDa
Detection of human SHP2 in immunoprecipitates of whole cell lysate from HeLa cells (1 mg for IP, 20% of IP loaded) using ab80611 at 3 µg/mg lysate for IP (Lane 1), and at 1 µg/ml for subsequent WB detection. Lane 2 represents control IgG IP. Detection: Chemiluminescence with an exposure time of 30 seconds.