Recombinant Human PTPN11 (SHP2) Protein

Name: Recombinant Human PTPN11 (SHP2) Protein
Brand: Beta LifeScience
SKU: BL-0152SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_002834
Synonym	SHP2, CFC, NS1, BPTP3, PTP2C, PTP-1D, SH-PTP2, SH-PTP3, MGC14433
Background	Mammalian PTPases can be subdivided into 1 of 2 broad categories: transmembrane receptor PTPases and intracellular PTPases. PTPN11 is one of the 2 closely related mammalian intracellular PTPases whose sequences encode 2 tandem SRC homology 2 (SH2) domains that are located at the amino-terminal side of a single PTPase catalytic domain (1). 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 (2)
Description	Recombinant full-length human PTPN11 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	98 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PTPN11 (SHP2) Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Protein-tyrosine phosphatase family, Non-receptor class 2 subfamily
Database References	HGNC: 9644 OMIM: 151100 KEGG: hsa:5781 STRING: 9606.ENSP00000340944 UniGene: PMID: 30108215 Authors identify that miR-186 serves as a tumor suppressor in OSCC. Downregulation of this microRNA may lead to a higher expression of oncogenic factor SHP2, which leads to activation of growth promoting signaling. PMID: 29407635 REVIEW: structural basis and recent research progression on SHP2 in various human disease, including genetic and cancer diseases. PMID: 27028808 the tumor promoting role of YAP is involved in SHP2 which functions as a tumor promoter in vitro but as a tumor suppressor in vivo PMID: 29699904 Data indicate that by inhibiting adenine nucleotide translocase 1 (ANT1) and mitochondrial dysfunction, tyrosine phosphatase SHP2 orchestrates an intrinsic regulatory loop to limit excessive NLR family, pyrin domain-containing 3 protein (NLRP3) inflammasome activation. PMID: 29255148 Findings revealed that SHP2 is associated with cisplatin-induced drug resistance in lung cancer and directly activates Ras, which in turn regulates the PI3K/Akt pathway. PMID: 29207183 SHP-2 is activated by CD16b crosslinking in neutrophils. PMID: 29137913 Proliferation and soft agar assays were used to demonstrate the functional contribution of SHP2 to cell growth and transformation. SHP2 expression correlated with SOX2 expression in glioma stem cell (GSC) lines and was decreased in differentiated cells. Forced differentiation of GSCs by removal of growth factors, as confirmed by loss of SOX2 expression, also resulted in decreased SHP2 expression. PMID: 28852935 PTPN11 plays a role in regulating neurotrophin protective signaling in neuronal cells; PTPN11 dysregulation promotes apoptotic activation. PMID: 28947394 This study provides information on phenotypes observed in Noonan syndrome patients with different PTPN11 mutations and defines two novel mutations. PMID: 26817465 SHP-2 protein may become a new target for anti-malignant transformation of glioma. PMID: 28620155 High SHP2 expression is associated with colorectal tumors. PMID: 27582544 SHP2 expression was activated by the HBx-NF-kappaB pathway. In patients with HCC, a loss of SHP2 expression was associated with suppressed NF-kappaB-SHP2-ERK pathway activity and accelerated HCC development, whereas SHP2 overexpression in parallel with increased STAT3 activity was associated with fibrosis promotion during the early stages of HCC development. PMID: 28460481 The inhibitory action of cryptotanshinone is largely attributed to the inhibition of STAT3 Tyr705 phosphorylation with a novel mechanism of upregulating the tyrosine phosphatase activity of SHP-2 protein. PMID: 28492557 Studies indicate that multiple classes of PTPN11 mutations with a distinct perturbing effect on SHP2's function. PMID: 28074573 Mutational status of NRAS, KRAS, and PTPN11 genes is associated with genetic/cytogenetic features in children with B-precursor acute lymphoblastic leukemia. PMID: 28853218 Studied mutations of PTPN11 in a cohort of Noonan Syndrome patients. Mutational analysis was performed and PTPN11 mutations were detected in 11 out of 17 (64.7%) patients with Noonan syndrome; 72% had mutation in exon 3 and 27 % had mutation in exon 13. PMID: 28607217 NO controls the calcium signal propagation through Cx37-containing gap junctions. The tyrosine phosphatase SHP-2 is the essential mediator and NO target. PMID: 29025706 we describe patients with craniosynostosis and Noonan syndrome due to de novo mutations in PTPN11 and patients with craniosynostosis and CFC syndrome due to de novo mutations in BRAF or KRAS. All of these patients had cranial deformities in addition to the typical phenotypes of CFC syndrome and Noonan syndrome. PMID: 28650561 These results suggest that SHP-2-via association with ICAM-1-mediates ICAM-1-induced Src activation and modulates VE-cadherin switching association with ICAM-1 or actin, thereby negatively regulating neutrophil adhesion to endothelial cells and enhancing their transendothelial migration. PMID: 28701303 High PTPN11 expression is associated with suppression of T lymphocyte function in Melanoma. PMID: 27930879 PTPN11 mutations are the most common cause of the Noonan syndrome, along with frequent neuroepithelial brain tumors. (Review) PMID: 28328117 A novel PTPN11 mutation defined in two separate fetuses with Cystic hygroma and associated with Noonan syndrome phenotype is being reported. PMID: 27193571 High PTPN11 expression is associated with Pancreatic cancer. PMID: 27213290 SHP-2 acts together with PI3K/AKT to regulate a ZEB1-miR-200 feedback loop in PDGFRalpha-driven gliomas. PMID: 27041571 The data presented in the current study reveal that intestinal serotonin transporter (SERT) 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 function. PMID: 28209599 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. PMID: 27736153 PTPN11 variant was identified in a case with a lethal presentation of Noonan syndrome. PMID: 28098151 Appropriate knowledge of the phenotype-genotype correlations and of the outcome of cochlear implantation in genetic hearing impairment is important in the work-up to a CI PMID: 28483241 our results provide strong evidence that CD244 co-operates with c-Kit to regulate leukemogenesis through SHP-2/p27 signaling. PMID: 28126968 SHP2, SOCS3 and PIAS3 levels are reduced in medulloblastomas in vivo and in vitro, of which PIAS3 downregulation is more reversely correlated with STAT3 activation. In resveratrol-suppressed medulloblastoma cells with STAT3 downregulation and decreased incidence of STAT3 nuclear translocation, PIAS3 is upregulated, the SHP2 level remains unchanged and SOCS3 is downregulated. PMID: 28035977 could promote hepatocellular carcinoma cell dedifferentiation and liver cancer stem cell expansion by amplifying beta-catenin signaling PMID: 28059452 The results revealed that although the expression levels of SOCS1, SOCS3 and, in particular, pSHP2, tend to decrease in the four types of astrocytomas, PIAS3 downregulation is more negatively correlated with STAT3 activation in the stepwise progress of astrocytomas and would indicate an unfavorable outcome. PMID: 28035384 In a retroviral transduction/transplantation mouse model, mice transplanted with MLL/AF10(OM-LZ) cells harboring PTPN11(wt) developed myelomonocytic leukemia. Those transplanted with cells harboring PTPN11(G503A) -induced monocytic leukemia in a shorter latency. Adding PTPN11(G503A) to MLL/AF10 affected cell proliferation, chemo-resistance, differentiation, in vivo BM recruitment/clonal expansion and faster progression. PMID: 27859216 Shp2 (Src-homology 2 domain-containing phosphatase 2) functions as a negative regulator for STAT3 transcription factor (Stat3) activation in esophageal squamous cell cancer (ESCC). PMID: 28085101 the phosphatase activity of Shp2 and its tyrosine phosphorylation, are necessary for the IL-6-induced downregulation of E-cadherin and the phosphorylation of Erk1/2. Our findings uncover an important function that links Shp2 to IL-6-promoted breast cancer progression. PMID: 28208810 This study reveals the critical contribution of Ptpn11 mutations in the bone marrow microenvironment to leukaemogenesis and identifies CCL3 as a potential therapeutic target for controlling leukaemic progression in Noonan syndrome and for improving stem cell transplantation therapy in Noonan-syndrome-associated leukaemias. PMID: 27783593 higher expression of SHP2 might be involved in the progression of pancreatic ductal adenocarcinoma, suggesting that SHP2 may be a potential prognostic marker and target for therapy PMID: 26695153 Data indicate that the most prominent proteins associating with Gab2 are PTPN11, PIK3R1 and ARID3B. PMID: 27025927 Since rs2301756 polymorphism of PTPN11 was associated with reduced risk of gastric cancer and better effects of chemotherapy on gastric cancer, it can be considered as a predictor of gastric cancer prognosis and the treatment target for gastric cancer. PMID: 27614952 SHP2 gain-of-function mutation enhances malignancy of breast carcinoma. PMID: 26673822 mutation in PTPN11 is associated with co-occurrence of hypertrophic cardiomyopathy and myeloproliferative disorder in a neonate with Noonan syndrome. PMID: 26286251 The existence of a tight association between SHP2 and EGFR expression in tumors and cell lines further suggested the importance of SHP2 in EGFR expression. PMID: 26728598 patients with low Shp2 expression exhibited superior prognosis to sorafenib PMID: 25865556 Combined X-ray crystallography, small-angle X-ray scattering, and biochemistry to elucidate structural and mechanistic features of three cancer-associated SHP2 variants with single point mutations within the N-SH2:PTP interdomain autoinhibitory interface. PMID: 27030275 In vitro assays suggested that LEOPARD syndrome-associated SHP-2 mutations might enhance melanin synthesis in melanocytes, and that the activation of Akt/mTOR signalling may contribute to this process. PMID: 25917897 SHP2 may promote invadopodia formation through inhibition of Rho signaling in cancer cells. PMID: 26204488 Shp2 promotes metastasis of prostate cancer by attenuating the PAR3/PAR6/aPKC polarity protein complex and enhancing epithelial-to-mesenchymal transition PMID: 26050620 PTPN11 is a central node in intrinsic and acquired resistance to targeted cancer drugs. PMID: 26365186 SHP2 preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signaling. PMID: 26617336

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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