Abcam, ab257194, Human MTAP knockout HeLa cell lysate

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MTAP KO cell lysate available now. KO validated by Western blot. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon1 and Insertion of the selection cassette in exon1.
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon1 and Insertion of the selection cassette in exon1.,
Disease:Adenocarcinoma

Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages

Properties and Storage Information:
Gene name-MTAP, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
MTAP also known as methylthioadenosine phosphorylase is an essential enzyme that breaks down 5'-methylthioadenosine (MTA) a byproduct of polyamine synthesis. MTAP has a molecular weight of about 31 kDa. The enzyme converts MTA into adenine and 5-methylthioribose-1-phosphate which re-enter the methionine and adenine salvage pathways. MTAP is widely expressed in most tissues but its activity is especially high in the liver and kidney. Alternative names for MTAP include 2G4 and MTAP-A.
Biological function summary
Methylthioadenosine phosphorylase plays a significant role in the salvage pathways for methionine and adenine critical for cellular growth and proliferation. MTAP operates as a part of a complex metabolic network involved in polyamine metabolism. In addition to its metabolic functions MTAP contributes to the regulation of the immune response and cell cycle. MTAP immunohistochemistry is often used to study its expression patterns in various tissues.
Pathways
Methylthioadenosine phosphorylase participates importantly in the polyamine biosynthesis and methionine salvage pathways. These pathways are integral for maintaining cellular homeostasis and nucleotide pools. MTAP works closely with proteins such as methionine adenosyltransferase (MAT) and adenosylmethionine decarboxylase (AMD). In concert they facilitate the regeneration of methionine highlighting MTAP's role in cellular adaptation to metabolic demands.
Methylthioadenosine phosphorylase deficiency or deletion is linked to certain cancers such as gliomas and lymphomas. Loss of MTAP function is often associated with co-deletion of the tumor suppressor protein p16INK4a observed in various malignancies. This deletion can lead to an accumulation of MTA creating a toxic environment that promotes cancer cell proliferation. MTAP and its interaction with proteins like p16INK4a highlight its relevance as a potential target for therapeutic intervention in cancer treatment programs.