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AB96231

Anti-MTAP antibody

4

(1 Review)

|

(3 Publications)

Rabbit Polyclonal MTAP antibody. Suitable for ICC/IF, WB, IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human MTAP.

View Alternative Names

MSAP, MTAP, S-methyl-5'-thioadenosine phosphorylase, 5'-methylthioadenosine phosphorylase, MTA phosphorylase, MTAPase

3 Images
Immunocytochemistry/ Immunofluorescence - Anti-MTAP antibody (AB96231)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-MTAP antibody (AB96231)

Immunofluorescence analysis of HeLa cells fixed in 4% paraformaldehyde at RT for 15 min labelling MTAP protein at cytoplasm and nucleus using ab96231 at a 1/500 dilution (Green).
Hoechst 33342 was used for nuclear staining (Blue).

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-MTAP antibody (AB96231)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-MTAP antibody (AB96231)

ab96231, at a 1/500 dilution, staining Human MTAP in SAS xenograft, using Immunohistochemistry, Formalin/PFA-fixed paraffin-embedded tissue.

Western blot - Anti-MTAP antibody (AB96231)
  • WB

Unknown

Western blot - Anti-MTAP antibody (AB96231)

12% SDS PAGE

All lanes:

Western blot - Anti-MTAP antibody (ab96231) at 1/1000 dilution

All lanes:

A431 whole cell lysate at 30 µg

Predicted band size: 31 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human MTAP. The exact immunogen used to generate this antibody is proprietary information.

Q13126

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
See full target information MTAP

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Cancer research communications 4:2133-2146 PubMed38994676

2024

Spatial Landscape of Malignant Pleural and Peritoneal Mesothelioma Tumor Immune Microenvironments.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaojun Ma,David Lembersky,Elena S Kim,Michael J Becich,Joseph R Testa,Tullia C Bruno,Hatice U Osmanbeyoglu

Journal of cellular and molecular medicine 24:5565-5577 PubMed32301278

2020

PRMT5 silencing selectively affects MTAP-deleted mesothelioma: In vitro evidence of a novel promising approach.

Applications

Unspecified application

Species

Unspecified reactive species

Marcella Barbarino,Daniele Cesari,Maria Bottaro,Luca Luzzi,Asadoor Namagerdi,Franca Maria Bertolino,Cristiana Bellan,Fabrizio Proietti,Pasquale Somma,Mariacarolina Micheli,Maria Margherita de Santi,Raffaella Guazzo,Luciano Mutti,Luigi Pirtoli,Piero Paladini,Paola Indovina,Antonio Giordano

Oncotarget 9:28625-28637 PubMed29983885

2018

RIOK1 kinase activity is required for cell survival irrespective of status.

Applications

Unspecified application

Species

Unspecified reactive species

Alexandra Hörmann,Barbara Hopfgartner,Thomas Köcher,Maja Corcokovic,Teresa Krammer,Christoph Reiser,Gerd Bader,Junwei Shi,Katharina Ehrenhöfer,Simon Wöhrle,Norbert Schweifer,Christopher R Vakoc,Norbert Kraut,Mark Pearson,Mark Petronczki,Ralph A Neumüller
View all publications

Product promise

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