|Product Name||Anti-SHP2/PTPN11 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Tyrosine-protein phosphatase non-receptor type 11(PTPN11) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-SHP2/PTPN11 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1114)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human SHP2(578-592aa EDSARVYENVGLMQQ), identical to the related rat and mouse sequences.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat
Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti-SHP2 antibody, PA1114, Western blotting
WB: JURKAT Cell Lysate
Anti-SHP2 antibody, PA1114, IHC(P)
IHC(P): Human Thyroid Cancer Tissue
Protein Target Info (Source: Uniprot.org)
|Protein Name||Tyrosine-protein phosphatase non-receptor type 11|
|Tissue Specificity||Widely expressed, with highest levels in heart, brain, and skeletal muscle. .|
|Alternative Names||Tyrosine-protein phosphatase non-receptor type 11;220.127.116.11;Protein-tyrosine phosphatase 1D;PTP-1D;Protein-tyrosine phosphatase 2C;PTP-2C;SH-PTP2;SHP-2;Shp2;SH-PTP3;PTPN11;PTP2C, SHPTP2;|
|Molecular Weight||68436 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. .|
|Research Areas||Auditory System, Neuroscience, Protein Phosphorylation, Sensory System, Signal Transduction, Tyrosine Phosphatases
*You can search these to find other products in these research areas.
|Background||The tyrosine phosphatase Shp2 is recruited into tyrosine-kinase signalling pathways through binding of its two amino-terminal SH2 domains to specific phosphotyrosine motifs, concurrent with its re-localization and stimulation of phosphatase activity. Shp2 can potentiate signalling through the MAP-kinase pathway and is required during early mouse development for gastrulation. Shp2 is specifically required in mesenchyme cells of the progress zone(PZ), directly beneath the distal ectoderm of the limb bud. Rather than integrating proliferative signals, Shp2 probably exerts its effects on limb development by influencing cell shape, movement or adhesion. Furthermore, the branchial arches, which also use Fgfs during bud outgrowth, similarly require Shp2. Thus, Shp2 regulates phosphotyrosine-signalling events during the complex ectodermal-mesenchymal interactions that regulate mammalian budding morphogenesis.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,