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AB126623

Anti-MTAP antibody [EPR6892]

5

(1 Review)

|

(3 Publications)

Rabbit Recombinant Monoclonal MTAP antibody. Suitable for WB and reacts with Mouse, Rat, Human samples. Cited in 3 publications.

View Alternative Names

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

1 Images
Western blot - Anti-MTAP antibody [EPR6892] (AB126623)
  • WB

Unknown

Western blot - Anti-MTAP antibody [EPR6892] (AB126623)

All lanes:

Western blot - Anti-MTAP antibody [EPR6892] (ab126623) at 1/1000 dilution

Lane 1:

HeLa (Human cervix adenocarcinoma epithelial cell) whole cell lysate at 20 µg

Lane 2:

Human heart lysate at 20 µg

Lane 3:

NIH/3T3 (Mouse embryonic fibroblast) whole cell lysate at 20 µg

Lane 4:

Mouse heart lysate at 20 µg

Lane 5:

C6 (Rat glial tumor glial cell) whole cell lysate at 20 µg

Lane 6:

Rat heart lysate at 20 µg

Secondary

All lanes:

Goat Anti-Rabbit IgG (HRP) with minimal cross-reactivity with human IgG at 1/2000 dilution

Predicted band size: 31 kDa

false

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR6892

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Rat, Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -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.

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

iScience 27:111290 PubMed39618500

2024

Broad and diverse roles of sphingosine-1-phosphate/sphingosine-1-phosphate receptors in the prostate.

Applications

Unspecified application

Species

Unspecified reactive species

Daoquan Liu,Jianmin Liu,Yan Li,Lu Du,Qingqiong Cao,Liang Yang,Yongying Zhou,Ping Chen,Yuming Guo,Guang Zeng,Michael E DiSanto,Weidong Hu,Xinhua Zhang

Molecular cancer research : MCR 20:244-252 PubMed34728552

2021

A Functional Precision Oncology Approach to Identify Treatment Strategies for Myxofibrosarcoma Patients.

Applications

Unspecified application

Species

Unspecified reactive species

Chantal Pauli,Lamberto De Boni,Jonathan E Pauwels,Yanjiang Chen,Lara Planas-Paz,Reid Shaw,Brooke M Emerling,Carla Grandori,Benjamin D Hopkins,Mark A Rubin

Nature communications 12:4228 PubMed34244484

2021

Homozygous MTAP deletion in primary human glioblastoma is not associated with elevation of methylthioadenosine.

Applications

Unspecified application

Species

Unspecified reactive species

Yasaman Barekatain,Jeffrey J Ackroyd,Victoria C Yan,Sunada Khadka,Lin Wang,Ko-Chien Chen,Anton H Poral,Theresa Tran,Dimitra K Georgiou,Kenisha Arthur,Yu-Hsi Lin,Nikunj Satani,Elliot S Ballato,Eliot I Behr,Ana C deCarvalho,Roel G W Verhaak,John de Groot,Jason T Huse,John M Asara,Raghu Kalluri,Florian L Muller
View all publications

Product promise

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For full details, please see our Terms & Conditions

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