Recombinant Human Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (PTEN)

Code CSB-YP018964HU
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Source Yeast
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Code CSB-EP018964HU
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Source E.coli
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Code CSB-EP018964HU-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-BP018964HU
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Source Baculovirus
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Code CSB-MP018964HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PTEN
Uniprot No.
Alternative Names
10q23del; BZS; DEC; GLM2; MGC11227; MHAM; MMAC1; MMAC1 phosphatase and tensin homolog deleted on chromosome 10; Mutated in multiple advanced cancers 1; Phosphatase and tensin homolog; Phosphatase and tensin like protein; Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; Pten; PTEN_HUMAN; PTEN1; TEP1
Species
Homo sapiens (Human)
Expression Region
2-403
Target Protein Sequence
TAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV
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.

Customer Reviews and Q&A

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 Q&A
Q:

I'm looking for Human PTEN recombinant protein (full-length) Do you have anything available ?

A:
Thanks for your inquiry. We can provide this full length protein, please check the detailed information listed as below:
Recombinant Human Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN(PTEN)
CSB-BP018964HU >> Baculovirus
Expression Region: 2-403aa; Full length of the mature protein.
Tag information: Tag type will be determined during the manufacturing process.
The expected tag is N-terminal 10xHis-tagged and C-terminal Myc-tagged.
Sequence:

TAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV

Target Background

Function
Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.; Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1.
Gene References into Functions
  1. Nuclear phosphatase and tensin homologue on chromosome ten protein (PTEN) interacts with the splicing machinery, spliceosome, to regulate its assembly and pre-mRNA splicing. PMID: 29921876
  2. the expression of PTEN and miR-144 was inversely correlated in metastatic breast cancer cell lines. PMID: 30132256
  3. Disruption of PTEN proteinisoform PTENbeta (PTENbeta) alters rDNA transcription and promotes ribosomal biogenesis. PMID: 28332494
  4. Functionally, Ataxin-3 overexpression promoted cell proliferation, and Ataxin-3 knockdown inhibited cell proliferation in testicular cancer cell. In addition, up-regulation of Ataxin-3 inhibited the expression of PTEN and activated the AKT/mTOR pathway. PMID: 29902454
  5. a certain degree of mitochondrial oxidative activity, with some difference for PTEN-wild type SF767 cells respect to PTEN-deleted A172 and U87MG characterized by a loss-of-function point mutation of PTEN. PMID: 29209894
  6. We demonstrated that expression of PTEN and miR-718 were significantly correlated in patients with gastric cancer. Low expression of PTEN and high level of miR-718 were notably associated with a lower 5-year overall survival rate. Both PTEN and miR-718 were identified as prognostic factors of gastric cancer. PMID: 30131483
  7. The data indicate that diagnostic or therapeutic chest radiation may predispose patients with decreased stromal PTEN expression to secondary breast cancer, and that prophylactic EGFR inhibition may reduce this risk. PMID: 30018330
  8. findings indicated that shikonin inhibits proliferation and promotes apoptosis in human endometrioid endometrial cancer (EEC) cells by modulating the miR-106b/PTEN/AKT/mTOR signaling pathway, suggesting shikonin could act a potential therapeutic agent in the EEC treatment. PMID: 29449346
  9. SIRT6 inhibited proliferation, migration, and invasion of colon cancer cells by up-regulating PTEN expression and down-regulating AKT1 expression. PMID: 29957460
  10. Data show that phosphatase and tensin homolog (PTEN) interacts with death domain associated protein (DAXX) and, in turn PTEN directly regulates oncogene expression by modulating DAXX-histone H3.3 (H3.3) association on the chromatin. PMID: 28497778
  11. Study suggested that there may be a regulatory loop between miR21 and PTEN, and that miR21 inhibition affected the proliferative, invasive and apoptotic abilities of oral squamous cell carcinoma (OSCC) cells. miR-21 expression was observed in 80.0% OSCC tissues and in 30.0% of normal tissues. By contrast, PTEN expression exhibited an opposite trend in OSCC tissues 37.1%, and normal tissues 80.0%. PMID: 30132571
  12. MTSS1 is stabilized by the protein phosphatase activity of the tumor suppressor PTEN. Our data show that PTEN loss in PDAC cells results in both increased metastatic potential and decreased MTSS1 expression. Furthermore, we show that ectopic MTSS1 expression rescues this effect. PMID: 29175021
  13. Low PTEN mRNA expression was associated with down-regulation of a group of genes involved in immune responses and B-cell development. PMID: 29734016
  14. Results showed that MiR-374b was highly expressed, while PTEN was downregulated in the GIST tissues. The levels of miR-374b, PI3K, AKT and PTEN were related to tumor diameter and pathological stage. Additionally, miR-374b increased the mRNA and protein levels of PI3K, Akt, MMP2, MMP9, P53 and cyclinD1, suggesting that miR-374b activates PI3K/Akt signaling pathway in GIST-T1 cells. PMID: 29902839
  15. PTEN loss is associated with castration-resistant prostate cancer. PMID: 29302046
  16. Low PTEN expression is associated with thyroid cancer progression. PMID: 30015900
  17. we provide a review on current understandings of the regulation of PTEN by ncRNAs, which could contribute to the development of novel approaches to the diseases with abnormal expression of PTEN. PMID: 30217221
  18. The IRIS-driven metastatic mechanism results from IRIS-dependent suppression of phosphatase and tensin homolog (PTEN) transcription, which in turn perturbs the PI3K/AKT/GSK-3beta pathway leading to prolyl hydroxylase-independent HIF-1alpha stabilization and activation in a normoxic environment. PMID: 30254159
  19. In this study, we used the Ion Personal Genome Machine (PGM) and Ion Torrent Ampliseq Cancer panel to sequence hotspot regions from PIK3CA, AKT and PTEN genes to identify genetic mutations in 39 samples of TNBC subtype from Moroccan patients and to correlate the results with clinical-pathologic data PMID: 30227836
  20. Data indicate a significant prognostic role for assessing transcriptional regulator ERG (ERG) and phosphatase and tensin homolog protein (PTEN) in men with prostate cancer. PMID: 30101374
  21. Low PTEN expression is associated with multiple myeloma. PMID: 30015974
  22. The loss of Sirt3 triggered fatal mitochondrial fission by suppressing the Akt/PTEN pathway. PMID: 30021354
  23. Results showed that SIX1 was overexpressed in osteosarcoma tissues, blood samples and cell lines, whereas PTEN expression was reduced. PMID: 29807230
  24. miR23b3p and PTEN interfered with the viability and apoptosis of smooth muscle cells. PMID: 29845190
  25. PDCD4 and PTEN were the functional targets of miR-21. PMID: 30074182
  26. miR-205 functions as an oncogenic miRNA by directly binding to SMAD4 and PTEN, providing a novel target for the molecular treatment of ovarian cancer. PMID: 28145479
  27. Studies have indicated that in breast cancer, PTEN undergo mutations. There is a functional and mechanistic link between the BMI-1 oncoprotein and tumor suppressor PTEN in the development and progression of breast cancer. [review] PMID: 30096458
  28. When considered together (43 cases), 1/25 cases (4%) with a PIK3CA mutation and/or low PTEN expression levels had a pathologic complete response (pCR)compared to 7/18 cases (39%) with wild-type PI3KCA and high PTEN expression levels (p = 0.006). PMID: 29110152
  29. Taken together, the authors presented here a novel cross-talk between miR-181a and PTEN which was raised by hepatitis B virus X protein, and this shined a new line in hepatitis B virus-related hepato-carcinogenesis. PMID: 28053323
  30. Bioinformatics analysis demonstrated that the 3'UTR of PTEN mRNA was targeted by hsa-miR-142-5p which regulates its expression triggering cancer stem cell-like properties of cutaneous squamous cell carcinoma. PMID: 28857248
  31. PTEN lipid phosphatase inactivation abolished the MOB1-LATS1/2 interaction, decreased YAP phosphorylation and finally promoted YAP nuclear translocation, which enhanced the synergistic effect of YAP-TEAD, thus inducing cell proliferation and migration. PMID: 30134988
  32. TERT could induce thyroid carcinoma cell proliferation mainly through the PTEN/AKT signaling pathway. PMID: 29901196
  33. These results suggest that miR214 mediates vascular inflammation and apoptosis via PTEN expression. PMID: 29916551
  34. A novel information on the susceptibility of PTEN to the inflammatory oxidant HOCl and its effects on the structure and activity of the protein is provided. PMID: 29298524
  35. Study proposes a new mechanism by which loss of PTEN and consequent activation of the PI3K-AKT-mTORC1-S6K1 signalling pathway impairs DNA repair by downregulation of MRE11. PMID: 28967905
  36. In prostate tumor tissue microarrays, loss of PTEN phosphohydrolase (PTEN) correlates with increased tyrosine kinase 6 PTK6 tyrosine 342 (PY342) phosphorylation and poor outcome. PMID: 29142193
  37. in silico analysis revealed PTEN to be the downstream target of miR-21, which was further confirmed by expression analysis. PMID: 29807978
  38. The decreased PTEN was associated with poorer survival outcomes of patients with kidney cancer and PTEN acts as a tumor suppressor in tumorigeneses and progression in kidney cancer. PMID: 29408173
  39. MiR-221 together with proteins MDR1 and ABCG2 was upregulated in Cisplatin-resistant A549 lung cancer cells. Anti-miR-221 inhibits proliferation and induces senescence in lung cancer cells. PTEN/Akt pathway axis was identified as a target of drug resistance induced by miR-221. PMID: 29876362
  40. These results demonstrate that SPAG6 silencing induces PTEN expression to regulate apoptosis though the PI3K/AKT pathway, indicating that SPAG6 may be a potential therapeutic target for myelodysplastic syndromes. PMID: 29749435
  41. The inhibition of PTEN also reduced the cancer effects of CD4+ T cells on non-small cell lung cancer (NSCLC) cell lines following miR-142-5p downregulation. Therefore, our study demonstrated that miR-142-5p regulated CD4+ T cells in human NSCLC through PD-L1 expression via the PTEN pathway. PMID: 29767245
  42. a statistically significant association between PTEN loss and the triple negative breast cancers was found in African American women PMID: 29653745
  43. miR-130b was upregulated in the lupus nephritis group, compared with that in the control group. PTEN was identified as a virtual target of miR-130b, and there was a negative regulatory association between miR-130b and PTEN. miR-130b and PTEN interfered with the viability and apoptosis of mesangial cells. PMID: 29620214
  44. The results of the present study indicate that the expression of miRNA23a may regulate acute myocardial infarction (AMI) through targeting PTEN in patients and in vitro, and PTEN/miRNA23a may therefore be potential targets for the clinical treatment of AMI. PMID: 29488607
  45. TRPC1 regulated HIF1alpha levels in PTEN-deficient MDA-MB-468 and HCC1569 breast cancer cell lines. This regulation arises from effects on the constitutive translation of HIF1alpha under normoxic conditions via an Akt-dependent pathway. PMID: 28559303
  46. miR367 was revealed to bind directly to phosphatase and tensin homolog (PTEN) mRNA and regulate the expression of the PTEN protein PMID: 29512776
  47. The present study confirmed that pAURKA is important in the development of gastric adenocarcinoma and revealed a novel functional link between PTEN, AURKA and pAURKA activation PMID: 29512701
  48. study found that CKS2 knockdown induced PTEN up-regulation and may associate with P53 pathway activation PMID: 29487004
  49. Study showed for the first time that the suppression of rheumatiod arthritis fibroblast-like synoviocyte was mediated by phosphatase and tensin homolog involving survivin silencing. PMID: 28337018
  50. The overexpression of PTEN concomitant with Livin gene silencing was confirmed as a feasible and effective in vitro and in vivo gene modulation method, which may represent a potential therapeutic strategy for the treatment of Gastric Cancer. PMID: 29436592

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Involvement in disease
Cowden syndrome 1 (CWS1); Lhermitte-Duclos disease (LDD); Bannayan-Riley-Ruvalcaba syndrome (BRRS); Squamous cell carcinoma of the head and neck (HNSCC); Endometrial cancer (ENDMC); Glioma 2 (GLM2); VACTERL association with hydrocephalus (VACTERL-H); Prostate cancer (PC); Macrocephaly/autism syndrome (MCEPHAS)
Subcellular Location
Cytoplasm. Nucleus. Nucleus, PML body.; [Isoform alpha]: Secreted. Note=May be secreted via a classical signal peptide and reenter into cells with the help of a poly-Arg motif.
Tissue Specificity
Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.
Database Links

HGNC: 9588

OMIM: 137800

KEGG: hsa:5728

STRING: 9606.ENSP00000361021

UniGene: Hs.500466

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