M1949
S-methyl-5′-thioadenosine phosphorylase human
recombinant
expressed in E. coli
Quality Level
Assay
≥80% (SDS-PAGE)
form
solution
relevant disease(s)
cancer
shipped in
dry ice
storage temp.
−70°C
General description
N-terminal GST-tagged 57 kDa protein containing amino acids 2-end.
Application
S-methyl-5′-thioadenosine phosphorylase human (MTAP) is an enzyme used in cancer research that is deficient in many types of cancer. Decreased MTAP expression may be used as a potential indicator of disease progression of gastrointestinal stromal tumors . MTAP may be a used to develop potential therapeutic strategies for hepatocellular carcinoma (HCC) since MTAP inactivation has been linked to HCC development and invasiveness .
Biochem/physiol Actions
MTAP expression is crucial for the catabolism of methylthioadenosine, which is a by-product of polyamine biosynthesis in the methionine salvage pathway. Protein expression is decreased by homozygous deletion and promoter hypermethylation .
Physical form
Supplied as a solution in 25 mM Tris-HCl, pH 8.0,100 mM NaCl, 0.05% Tween®-20, 10% glycerol,and 3 mM DTT.
Legal Information
TWEEN is a registered trademark of Croda International PLC
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Giovanna Cacciapuoti et al.
Biochimica et biophysica acta, 1814(10), 1358-1366 (2011-06-21)
Purine nucleoside metabolism in the archaeon Pyrococcus furiosus is catalyzed by purine nucleoside phosphorylase (PfPNP) and 5'-deoxy-5'-methylthioadenosine phosphorylase (PfMTAP). These enzymes, characterized by 50% amino acid sequence identity, show non-common features of thermophilicity and thermostability and are stabilized by intramolecular
Zarah Glad Zimling et al.
Histopathology, 60(6B), E96-105 (2012-03-08)
Malignant pleural mesothelioma (MPM) often causes diagnostic difficulties for pathologists. We assessed whether loss of methylthioadenosine phosphorylase (MTAP), a key enzyme in the intracellular recycling of adenosine triphosphate (ATP) often deleted in MPM, could be detected with immunohistochemistry (IHC) and
Promoter-hypermethylation is causing functional relevant downregulation of methylthioadenosine phosphorylase (MTAP) expression in hepatocellular carcinoma
Claus Hellerbrand, Marcus Muhlbauer, et al.
Molecular Pharmacology, 52, 64-72 (2006)
Tony W H Li et al.
Carcinogenesis, 33(2), 427-435 (2011-12-14)
Chronic inflammation is an underlying risk factor for colon cancer. Tumor necrosis factor alpha (TNF-α) plays a critical role in the development of inflammation-induced colon cancer in a mouse model. S-adenosylmethionine (SAMe) and its metabolite methylthioadenosine (MTA) can inhibit lipopolysaccharide-induced
Jin Kim et al.
Genes, chromosomes & cancer, 50(6), 421-433 (2011-03-18)
The methylthioadenosine phosphorylase (MTAP) gene is located on 9p21 telomeric to the CDKN2A tumor suppressor gene. Loss of MTAP gene is frequently associated with CDKN2A homozygous deletion. Although the homozygous deletion of MTAP has been reported in various human cancers
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