Recombinant Rat Tyrosine-protein phosphatase non-receptor type 11 (Ptpn11)

Code CSB-YP019025RA
MSDS
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Source Yeast
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Code CSB-EP019025RA
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Source E.coli
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Code CSB-EP019025RA-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP019025RA
MSDS
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Source Baculovirus
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Code CSB-MP019025RA
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Ptpn11
Uniprot No.
Alternative Names
Ptpn11; Tyrosine-protein phosphatase non-receptor type 11; EC 3.1.3.48; Protein-tyrosine phosphatase 1D; PTP-1D; Protein-tyrosine phosphatase SYP; SH-PTP2; SHP-2; Shp2
Species
Rattus norvegicus (Rat)
Expression Region
2-597
Target Protein Sequence
TSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDSKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV ERGKSKCVKY WPDECALKEY GVMRVRNVRE SAAHDYTLRE LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ ESIVDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity. Dephosphorylates CDC73. Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification.
Gene References into Functions
  1. the effect of SHP-2 on the proliferation, cell cycle and apoptosis of renal tubular epithelial cells was investigated. PMID: 29991025
  2. Data demonstrate that the increased activation of MAPK signaling pathway by SHP2D61G could deregulate the surface expression of synaptic receptors during neuronal development. PMID: 28366775
  3. findings demonstrate that IL-17 regulates SHP-2 expression and IL-17RA/STAT-3 dependent production of Cyr61, IL-23, GM-CSF and RANKL in AA-FLS and may reveal a new insight into the pathogenesis of RA. PMID: 28898718
  4. 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(P)845 GluA1 and surface expression of GluA1 during synaptic scaling. (Shp2/Ptpn11 = protein tyrosine phosphatase non-receptor type 11; GluA1 = glutamate receptor ionotropic Ampa1 [alpha 1]) PMID: 28768764
  5. results have revealed a regulatory mechanism of Shp2 underlying LTP and memory, broadening our understanding of Shp2 in cognitive function. PMID: 27417137
  6. PKA phosphorylation of Shp2 protein inhibits its phosphatase activity and modulates ligand specificity PMID: 25802336
  7. Data indicate that protein tyrosine phosphatases SHP-1, SHP-2 and PTP1B overexpressed during the development of cerulein -induced acute pancreatitis can be modulated by extracellular signal-regulated kinases (ERK1/2) and c-Jun NH2-terminal kinase (JNK). PMID: 24225419
  8. our data show that in hemiparkinsonian rats developing dyskinesia, the aberrant phosphorylation of Shp-2 by D1R activation, represents an upstream molecular event leading to the persistent phosphorylation of Erk1/2 PMID: 23328768
  9. key regulator of blood-testis barrier integrity and Sertoli cell support of spermatogenesis and fertility PMID: 23325809
  10. Data indicate that the two LEOPARD syndrome mutations Q510E-Shp2 and Y279C-Shp2 both induce neonatal cardiomyocytes hypertrophy through similar mechanisms. PMID: 23673659
  11. changes in mitochondria-localized signaling molecules Src and SHP2 constitute a potential signaling pathway to affect mitochondrial dysfunction in the heart during sepsis PMID: 22952679
  12. These results indicate that SHP2 is recruited in focal adhesions of neural stem cells and regulates focal adhesion formation PMID: 22118986
  13. The results have revealed that Shp2 functions as an intracellular inhibitor of apoptosis. These data provide insight into the pathogenesis of heart diseases. PMID: 22537548
  14. the involvement of SHP2 activity in the regulation of the expression of the fatty acid-metabolizing enzyme ACSL4 PMID: 21903867
  15. SHP-2 promotes oligodendrocytes maturation via Akt and ERK1/2 signaling in vitro. PMID: 21701583
  16. SPRED1 is a likely substrate of SHP2, whose tyrosine dephosphorylation is required to attenuate the inhibitory action of SPRED1 in the Ras/ERK pathway. PMID: 21531714
  17. SHP2 supports basal pulmonary endothelial barrier function by coordinating the tyrosine phosphorylation profile of VE-cadherin, beta-catenin, and p190RhoGAP and the activity of RhoA. PMID: 20023173
  18. SHP-2 has a role as a positive regulator of cytokine receptor signaling by regulating ubiquitination/degradation pathways PMID: 14522994
  19. Shp-1 and Shp-2 are recruited on cell membrane in two distinct molecular complexes including Ret oncogenes PMID: 15115663
  20. first tyrosine phosphatase shown to be present in mitochondria PMID: 15378208
  21. These results demonstrate a unique role for SHP-2 in the regulation of the cellular architecture of vascular smooth muscle cells, suggesting the possibility that this phosphatase might be instrumental in vascular remodeling. PMID: 16021628
  22. ROS-mediated oxidation of SHP-2 is essential for HB-EGF-mediated EGFR transactivation in ET-1 signaling pathway in NRK-52E cells. PMID: 16261333
  23. studies demonstrate that SHP-1 & SHP-2 are expressed in myometrium & appear to be responsible for tyrosine phosphatase activity in this tissue, providing a molecular mechanism for modulation of phospholipase C-gamma1 phosphotyrosine levels in the uterus PMID: 16814162
  24. Tyr-542 of SHP-2 modulates IL-1-induced Ca2+ signals and association of the ER with focal adhesions PMID: 16905534
  25. Shp2 participates to the opposite effects induced in PC12 cells by EGF and NGF and that the interactions with the multidocking Gab2 protein mediate such effects. PMID: 17287109
  26. Our results show that AP is associated with increases in the expression of SHP-1 and SHP-2 and changes in the dynamics of SHP-2 subcellular distribution in the early phase of Cer-induced AP. PMID: 18294464
  27. Findings do not support an essential role of SHP2 in the pathogenesis of experimental pneumoniae meningitis, but it is possible that SHP2 protein expression may be used as a marker of disease activity. PMID: 18305318
  28. SHP-2 dysregulation by increased Nox1-derived ROS in spontaneously hypertensive rats is associated with altered Ang II-AKT signaling. PMID: 18566342
  29. Localization of PTP-1B, SHP-2, and Src exclusively in rat brain mitochondria and functional consequences.( PMID: 18583343
  30. Results indicate that a presynaptic signaling pathway through p120ctn, Fer, SHP-2, and beta-catenin promotes excitatory synapse development and function. PMID: 19047464
  31. ROS-mediated oxidation of SHP-2 is essential for the hUII-induced mitogenic pathway in NRK-52E cells. PMID: 19326266
  32. The SHP-2 is activated by ROS-mediated oxidative stress in astrocytes and functions as a component of the raft-mediated signaling pathway that acts through dephosphorylation and inactivation of other phosphotyrosine proteins, such as STAT-3. PMID: 19348936
  33. Report role for Gab1/SHP2 in thrombin activation of PAK1: gene transfer of kinase-dead PAK1 inhibits injury-induced restenosis. PMID: 19359598
  34. SHP-2 associated with Gab2 in rat basophilic leukemia cells; its association with Gab2 is enhanced following multimerization of FcERI and/or depolymerization of the filamentous actin. PMID: 15162432

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Subcellular Location
Cytoplasm.
Protein Families
Protein-tyrosine phosphatase family, Non-receptor class 2 subfamily
Tissue Specificity
Expressed in brain, muscle and lung.
Database Links
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