Analytical Data
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Gene name
MTAP
- Application
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Alternative Names
MTAP；MSAP；S-methyl-5'-thioadenosine phosphorylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P78559
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Expression Region
全长
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AA Sequence
full
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MTAP (methylthioadenosine phosphorylase) is an enzyme involved in purine metabolism and the salvage pathway of methylthioadenosine, a byproduct of the polyamine synthesis pathway. Research has indicated that MTAP is frequently deleted in a variety of cancers, particularly in tumor types with a high frequency of 9p21 deletion, which also includes the tumor suppressor genes CDKN2A and CDKN2B. The loss of MTAP expression correlates with poor prognosis due to the accumulation of toxic metabolites, leading to increased tumor growth and resistance to certain therapies. As a result, MTAP has gained attention as a potential therapeutic target. The development of MTAP recombinant proteins aims to better understand its enzymatic function and regulatory mechanisms, provide insights into its role in cancer biology, and potentially guide the creation of targeted therapeutic strategies. Furthermore, these recombinant proteins can be used in high-throughput screening assays to identify small molecules that may restore MTAP activity, thereby addressing the metabolic vulnerabilities of MTAP-deficient tumors. Understanding the structure-function relationship of MTAP through recombinant protein studies could also facilitate the design of enzyme inhibitors that selectively target cancer cells with MTAP loss, paving the way for novel treatment options.
