MMAC1 phosphatase and tensin homolog deleted on chromosome 10
Mutated in multiple advanced cancers 1
Background Information
The protein and lipid phosphatase PTEN (phosphatase and tensin homolog deleted on chromosome ten) has been suggested to play a role in tumorgenesis. PTEN is a tumor suppressor whose loss permits constitutive signaling through the PI3K pathway and is sufficient to cause cancer. In normal cells, in conjunction with FOXO1A and PTEN function together to restrain cell growth. PTEN metabolizes the product of PI3K phosphorylation of PI(4,5)P2 following receptor activation, creating PI(3,4,5)P3. In cells lacking PTEN, there are elevated levels of PI(3,4,5)P3, which acts as a potent second messenger promoting oncogenesis. Restoration of PTEN function is considered a novel approach to cancer therapy. Overexpression of PTEN inhibits cell migration, and expression of antisense PTEN mRNA enhances migration.
Product Information
Format
Unpurified
Control
NIH/3T3 cell lysate
Presentation
Rabbit Monoclonal in buffer containing tissue culture supernatant with 0.1% sodium azide and 0.05% BSA.
Applications
Application
Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target. Detect phospho-PTEN (Ser380) using this Anti-phospho-PTEN (Ser380) Antibody, clone EP2138Y, Rabbit validated for use in WB, IH(P) & IC.
Key Applications
Immunocytochemistry
Western Blotting
Immunohistochemistry (Paraffin)
Application Notes
Immunohistochemistry Analysis: A 1:100-250 dilution from a previous lot detected PTEN in human adenocarcinoma of uterus tissue.
Immunocytochemistry Analysis: A 1:100-250 dilution from a previous lot was used in IC.
Biological Information
Immunogen
Synthetic peptide corresponding to residues near Ser380 of human PTEN.
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 AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. CATALYTIC ACTIVITY:Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
A phosphoprotein + H2O = a protein + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. COFACTOR:Magnesium. SUBUNIT STRUCTURE:Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5. Interaction with MAGI2 increases protein stability. Interacts with NEDD4. Interacts (via C2 domain) with FRK. SUBCELLULAR LOCATION:Cytoplasm TISSUE SPECIFICITY:Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas. INDUCTION:Down-regulated by transforming growth factor beta (TGF-beta). DOMAIN:The C2 domain binds phospholipid membranes in vitro in a Ca2+-independent manner; this binding is important for its tumor suppressor function. PTM:Phosphorylated in vitro by MAST1, MAST2 and MAST3. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4. INVOLVEMENT IN DISEASE:Mutations of PTEN are found in a large number of cancers.
Defects in PTEN are a cause of Cowden disease (CD) [MIM:158350]; also known as Cowden syndrome (CS). CD is an autosomal dominant cancer predisposition syndrome associated with elevated risk for tumors of the breast, thyroid and skin. The predominant phenotype for CD is multiple hamartoma syndrome, in many organ systems including the breast (70% of CD patients), thyroid (40-60%), skin, CNS (40%), gastrointestinal tract. Affected individuals are at an increased risk of both breast and thyroid cancers. Trichilemmomas (benign tumors of the hair follicle infundibulum), and mucocutaneous papillomatosis (99%) are hallmarks of CD.
Defects in PTEN are the cause of Lhermitte-Duclos disease (LDD) [MIM:158350]; also known as cerebelloparenchymal disorder VI. LDD is characterized by dysplastic gangliocytoma of the cerebellum which often results in cerebellar signs and seizures. LDD and CD seem to be the same entity, and are considered as hamartoma-neoplasia syndromes.
Defects in PTEN are a cause of Bannayan-Zonana syndrome (BZS) [MIM:153480]; also known as Ruvalcaba-Myhre-Smith syndrome (RMSS) or Bannayan-Riley-Ruvalcaba syndrome (BRRS). In BZS there seems not to be an increased risk of malignancy. It has a partial clinical overlap with CD. BZS is characterized by the classic triad of macrocephaly, lipomatosis and pigmented macules of the gland penis.
Defects in PTEN are a cause of head and neck squamous cell carcinomas (HNSCC) [MIM:275355]; also known as squamous cell carcinoma of the head and neck.
Defects in PTEN are a cause of susceptibility to endometrial cancer [MIM:608089].
Defects in PTEN are a cause of Proteus syndrome [MIM:176920]. Proteus syndrome is a hamartomatous disorder characterized by overgrowth of multiple tissues, connective tissue and epidermal naevi, and vascular malformations. These presentations are usually apparent at birth or soon after and continue to develop as the patient ages. It is named after the Greek god Proteus who, legend has it, could change his shape at will to avoid capture. Tumors, mostly benign but some malignant, have also been reported in Proteus syndrome, generally presenting by the age of 20 years and including papillary adenocarcinoma of the testis, meningioma, and cystadenoma of the ovaries.
Defects in PTEN are a cause of oligodendroglioma [MIM:137800]; also called oligodendroblastoma or familial glioma of brain. Oligodendroglioma is a usually benign neoplasm derived from and composed of oligodendrogliocytes in varying stages of differentiation. The majority are seen in adults in the white matter of the brain.
Defects in PTEN are a cause of VACTERL association with hydrocephalus [MIM:276950]; which includes also VATER association with hydrocephalus. VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects.
Defects in PTEN are involved in prostate cancer [MIM:176807].
Defects in PTEN are a cause of macrocephaly/autism syndrome [MIM:605309]. Patients have autism spectrum disorders and macrocephaly, with head circumferences ranging from +2.5 to +8 SD for age and sex (average head circumference +4.0 SD).
A microdeletion of chromosome 10q23 involving PTEN and BMPR1A is a cause of chromosome 10q23 deletion syndrome [MIM:612242]. This syndrome shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome. SEQUENCE SIMILARITIES:Contains 1 C2 tensin-type domain.
Contains 1 phosphatase tensin-type domain.
Product Usage Statements
Quality Assurance
Evaluated by Western Blot on NIH/3T3 cell lysates.
Western Blot Analysis: A 1:1,000-2,000 dilution of this antibody was used to detect PTEN in NIH/3T3 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
MMAC1 phosphatase and tensin homolog deleted on chromosome 10
Mutated in multiple advanced cancers 1
Background Information
The protein and lipid phosphatase PTEN (phosphatase and tensin homolog deleted on chromosome ten) has been suggested to play a role in tumorgenesis. PTEN is a tumor suppressor whose loss permits constitutive signaling through the PI3K pathway and is sufficient to cause cancer. In normal cells, in conjunction with FOXO1A and PTEN function together to restrain cell growth. PTEN metabolizes the product of PI3K phosphorylation of PI(4,5)P2 following receptor activation, creating PI(3,4,5)P3. In cells lacking PTEN, there are elevated levels of PI(3,4,5)P3, which acts as a potent second messenger promoting oncogenesis. Restoration of PTEN function is considered a novel approach to cancer therapy. Overexpression of PTEN inhibits cell migration, and expression of antisense PTEN mRNA enhances migration.
Product Information
Format
Unpurified
Control
NIH/3T3 cell lysate
Presentation
Rabbit Monoclonal in buffer containing tissue culture supernatant with 0.1% sodium azide and 0.05% BSA.
Applications
Application
Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target. Detect phospho-PTEN (Ser380) using this Anti-phospho-PTEN (Ser380) Antibody, clone EP2138Y, Rabbit validated for use in WB, IH(P) & IC.
Key Applications
Immunocytochemistry
Western Blotting
Immunohistochemistry (Paraffin)
Application Notes
Immunohistochemistry Analysis: A 1:100-250 dilution from a previous lot detected PTEN in human adenocarcinoma of uterus tissue.
Immunocytochemistry Analysis: A 1:100-250 dilution from a previous lot was used in IC.
Biological Information
Immunogen
Synthetic peptide corresponding to residues near Ser380 of human PTEN.
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 AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. CATALYTIC ACTIVITY:Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
A phosphoprotein + H2O = a protein + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. COFACTOR:Magnesium. SUBUNIT STRUCTURE:Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5. Interaction with MAGI2 increases protein stability. Interacts with NEDD4. Interacts (via C2 domain) with FRK. SUBCELLULAR LOCATION:Cytoplasm TISSUE SPECIFICITY:Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas. INDUCTION:Down-regulated by transforming growth factor beta (TGF-beta). DOMAIN:The C2 domain binds phospholipid membranes in vitro in a Ca2+-independent manner; this binding is important for its tumor suppressor function. PTM:Phosphorylated in vitro by MAST1, MAST2 and MAST3. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4. INVOLVEMENT IN DISEASE:Mutations of PTEN are found in a large number of cancers.
Defects in PTEN are a cause of Cowden disease (CD) [MIM:158350]; also known as Cowden syndrome (CS). CD is an autosomal dominant cancer predisposition syndrome associated with elevated risk for tumors of the breast, thyroid and skin. The predominant phenotype for CD is multiple hamartoma syndrome, in many organ systems including the breast (70% of CD patients), thyroid (40-60%), skin, CNS (40%), gastrointestinal tract. Affected individuals are at an increased risk of both breast and thyroid cancers. Trichilemmomas (benign tumors of the hair follicle infundibulum), and mucocutaneous papillomatosis (99%) are hallmarks of CD.
Defects in PTEN are the cause of Lhermitte-Duclos disease (LDD) [MIM:158350]; also known as cerebelloparenchymal disorder VI. LDD is characterized by dysplastic gangliocytoma of the cerebellum which often results in cerebellar signs and seizures. LDD and CD seem to be the same entity, and are considered as hamartoma-neoplasia syndromes.
Defects in PTEN are a cause of Bannayan-Zonana syndrome (BZS) [MIM:153480]; also known as Ruvalcaba-Myhre-Smith syndrome (RMSS) or Bannayan-Riley-Ruvalcaba syndrome (BRRS). In BZS there seems not to be an increased risk of malignancy. It has a partial clinical overlap with CD. BZS is characterized by the classic triad of macrocephaly, lipomatosis and pigmented macules of the gland penis.
Defects in PTEN are a cause of head and neck squamous cell carcinomas (HNSCC) [MIM:275355]; also known as squamous cell carcinoma of the head and neck.
Defects in PTEN are a cause of susceptibility to endometrial cancer [MIM:608089].
Defects in PTEN are a cause of Proteus syndrome [MIM:176920]. Proteus syndrome is a hamartomatous disorder characterized by overgrowth of multiple tissues, connective tissue and epidermal naevi, and vascular malformations. These presentations are usually apparent at birth or soon after and continue to develop as the patient ages. It is named after the Greek god Proteus who, legend has it, could change his shape at will to avoid capture. Tumors, mostly benign but some malignant, have also been reported in Proteus syndrome, generally presenting by the age of 20 years and including papillary adenocarcinoma of the testis, meningioma, and cystadenoma of the ovaries.
Defects in PTEN are a cause of oligodendroglioma [MIM:137800]; also called oligodendroblastoma or familial glioma of brain. Oligodendroglioma is a usually benign neoplasm derived from and composed of oligodendrogliocytes in varying stages of differentiation. The majority are seen in adults in the white matter of the brain.
Defects in PTEN are a cause of VACTERL association with hydrocephalus [MIM:276950]; which includes also VATER association with hydrocephalus. VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects.
Defects in PTEN are involved in prostate cancer [MIM:176807].
Defects in PTEN are a cause of macrocephaly/autism syndrome [MIM:605309]. Patients have autism spectrum disorders and macrocephaly, with head circumferences ranging from +2.5 to +8 SD for age and sex (average head circumference +4.0 SD).
A microdeletion of chromosome 10q23 involving PTEN and BMPR1A is a cause of chromosome 10q23 deletion syndrome [MIM:612242]. This syndrome shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome. SEQUENCE SIMILARITIES:Contains 1 C2 tensin-type domain.
Contains 1 phosphatase tensin-type domain.
Product Usage Statements
Quality Assurance
Evaluated by Western Blot on NIH/3T3 cell lysates.
Western Blot Analysis: A 1:1,000-2,000 dilution of this antibody was used to detect PTEN in NIH/3T3 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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