Thymalin (10mg) 
5-amino-1mq
Price range: $50.00 through $190.00
Description
A single-component research material supplied for controlled research environments. 5-amino-1MQ (5 mg) is a small-molecule compound studied for its role as a selective NNMT (nicotinamide N-methyltransferase) inhibitor in metabolic and cellular energy research.
Composition
• 5-amino-1MQ
• Appearance: Lyophilized powder in a sealed research vial
Research Focus (non-clinical)
• Investigation of NNMT inhibition and its downstream metabolic effects
• Studies on NAD+ metabolism and energy homeostasis in preclinical models
• Development of analytical methods (HPLC/LC-MS) for small-molecule quantitation
• Stability and solubility assessment of 5-amino-1MQ under laboratory storage conditions
For qualified research professionals and institutional laboratories. Not for human use.
Documentation & Quality Assurance
Each lot is sourced through our verified global supply chain with emphasis on traceability and quality control. We work diligently to obtain and maintain third-party analytical reports (HPLC/LC-MS) and Certificates of Analysis for each batch, as part of our ongoing quality process. These documents are reviewed internally and displayed as they become available. Independent third-party testing is also performed on select lots to confirm identity, purity, and alignment with our internal specifications.
Important Notice
This product is intended for laboratory research use only. It is not intended for human or veterinary use, and must not be used for diagnostic, therapeutic, or clinical purposes.
This material is not a drug, medical device, or dietary supplement, and has not been evaluated by the U.S. Food and Drug Administration.
Quality & Manufacturing
All materials are sourced from carefully vetted domestic and international manufacturing partners who follow quality systems consistent with ISO and cGMP principles. Each supplier is reviewed for reliability, documentation integrity, and transparency in testing.
We require a verified purity of 99% or higher and perform independent third-party spot testing to confirm that select lots meet our internal standards for identity, purity, and composition. Where available, endotoxin testing results are included on Certificates of Analysis to verify laboratory purity; their inclusion is for research quality assessment only and does not imply suitability for human or veterinary use.
All research materials are sealed for integrity and packaged for stability during storage and transport from manufacturing through final delivery.
Additional information
| Weight | 0.2 lbs |
|---|---|
| Dosage | 5mg, 50mg |
Storage Instructions
All our research peptides are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.
Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.
Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.
Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.
⚠️ Important Notice: These products are intended for research use only. Not for human consumption.
Certificate of Analysis
Every batch undergoes rigorous third-party laboratory testing to verify identity, purity (≥98%), and quality before release.
All Available COAs
Research Use Only
These studies reference research-grade peptides for laboratory and scientific investigation only. Not for human consumption. Not intended to diagnose, treat, cure, or prevent any disease.
Published Scientific Research
Peer-reviewed laboratory research investigating research peptides from leading scientific databases
De novo design of peptide binders to conformationally diverse targets with contrastive language modeling.
In total, PepPrCLIP empowers the modulation of previously inaccessible proteins without reliance on stable and ordered tertiary structures.
View Full StudyProlonging parathyroid hormone analog action in vitro and in vivo through peptide lipidation.
Rapid clearance from the circulation and short dwell times on the PTH receptor limit the efficacies of conventional PTH peptides currently in medical use. Second, we append a lipid chain to a lysine side chain in a fashion designed to anchor the peptide to the cell membrane as the ligand is bound to the receptor and hence increase its dwell time on the receptor.
View Full StudyA comprehensive database of cheese-derived bitter peptides and correlation to their physical properties.
Bitterness is a common flavor attribute of aged cheese associated with the peptide fraction, but excessive levels are a defect leading to consumer rejection. Bitterness in cheese has been primarily associated with peptides that arise from the breakdown of casein.
View Full StudyStructurally manipulated antioxidant peptides derived from wheat bran: Preparation and identification.
The obtained peptides exhibited great antioxidant activities against HO-induced oxidative stress in HepG2 cells. The results revealed that peptides DLDW and DLGL demonstrated the highest binding affinities, and a bridge was formed between Asp of DLGL and Arg415 of Klech domain, contributing to interfering Keap1-Nrf2 interaction.
View Full StudyRapid and Quantitative Enrichment of Peptides from Plasma for Mass Spectrometric Analysis.
Quantitative analyses of peptides using the described method showed good correlation with existing immunoassays.
View Full StudyStructural modeling of peptide toxin-ion channel interactions using RosettaDock.
Peptidic toxins from animal venoms target ion channels and provide useful scaffolds for the rational design of novel channel modulators with enhanced potency and subtype selectivity. We tested this approach on 10 structures of peptide toxin-ion channel complexes and demonstrated that it can sample near-native structures in all tested cases.
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