Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated SHP2. The final product is generated by affinity chromatography using a SHP2 derived peptide that is phosphorylated at tyrosine 542.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/1000. Detects a band of approximately 70 kDa.
Not tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
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.
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
Western blot - SHP2 (phospho Y542) antibody (ab17939)
Predicted band size : 70 kDa
Western blot using ab17939 on 10-30µg NIH3T3 cell lysate.
Lane 1: untreated cells.
Lane 2: cells treated with PDGF.
Lane 3: cells treated with PDGF. Antibody blocked with non-phosphorylated immunopeptide.
Lane 4: cells treated with PDGF. Antibody blocked with a generic tyrosine-phosphorylated peptide.
Lane 5: cells treated with PDGF. Antibody blocked with phosphorylated immunopeptide.
Svensson KJ et al. Exosome uptake depends on ERK1/2-heat shock protein 27 signaling and lipid Raft-mediated endocytosis negatively regulated by caveolin-1. J Biol Chem288:17713-24 (2013).
Read more (PubMed: 23653359) »
Banes-Berceli AK et al. Angiotensin II and endothelin-1 augment the vascular complications of diabetes via JAK2 activation. Am J Physiol Heart Circ Physiol293:H1291-9 (2007).
Read more (PubMed: 17526654) »