Spermidine Phosphate TCI P2957 is a biochemical compound widely used in protein research and laboratory applications. This compound serves as a molecular modulator, playing a crucial role in stabilizing proteins and regulating enzymatic activity. It is an essential reagent for researchers aiming to understand and manipulate biological processes at the molecular level. Its ability to interact with proteins makes it a valuable tool in biochemical studies, supporting a wide range of experimental protocols.
One of the key properties that make Spermidine Phosphate a preferred choice is its chemical stability and compatibility with various experimental conditions. It maintains its structural integrity under normal laboratory conditions, ensuring consistent results across experiments. Additionally, its ability to specifically interact with proteins allows for precise control over biological functions, making it ideal for advanced research. The compound’s versatility and reliability have made it a staple in many research laboratories.
In Indonesian laboratories, Spermidine Phosphate is commonly used in biomedical and pharmacological research. It is particularly favored for its role in stabilizing proteins during storage and testing, ensuring the accuracy and reproducibility of experimental outcomes. Its presence in biological systems also makes it relevant for studies on cellular mechanisms, apoptosis, and molecular interactions. This compound is an essential component of many research protocols in the life sciences.
Advantages (TCI brochure)
- Polyamines can effectively stabilize biomolecules
- Reported to inhibit heat-induced aggregation of lysozyme
- Retained high lysozyme activity after heating at 98°C with 100 mM addition
TCI brochures (PDF)
- Protein Stabilizers 2024-09-26 · p. 1
- Protein and Biological Sample Preparation Reagents 2026-09-10 · p. 3
- Reagents for Biological Research 2025-03-11 · p. 23
Related TCI products
- TCI P3082 333-93-7 Putrescine Dihydrochloride [for Protein Research]
- TCI P2950 306-67-2 Spermine Tetrahydrochloride [for Protein Research]
- TCI A3531 26340-89-6 H-Arg-OMe.2HCl [for Protein Research]
- TCI S0385 49721-50-8 Spermidine Phosphate Hexahydrate
- TCI S0068 259244-14-9 Spermidine Phosphate
- TCI P3255 124-20-9 Spermidine
- Protein stabilization during storage and testing is enhanced by Spermidine Phosphate’s ability to maintain structural integrity of biomolecules.
- Enzymatic activity regulation benefits from its role as a molecular modulator, allowing precise control over biochemical reactions.
- Apoptosis research utilizes its interaction with cellular pathways, aiding in the study of programmed cell death mechanisms.
- Molecular interaction studies benefit from its specific binding properties, enabling detailed analysis of protein-protein and protein-ligand interactions.
- Biomedical research leverages its presence in biological systems to explore cellular mechanisms and disease-related processes.
From the TCI brochure
- Preventing aggregation of target proteins
- Protein stabilization
| Brand | TCI |
|---|---|
| CAS number | 259244-14-9 |
| Molecular formula | — |
| Purity | — |
| Category | Life Science > Biochemicals and Reagents > Stabilization of Biomolecules |
| Pack sizes | — |
| Physical form | — |
| Storage | Store in a cool, dry place away from direct sunlight |
Spermidine Phosphate should be stored in a cool, dry environment to maintain its chemical stability. It is recommended to keep the compound in a sealed container to prevent moisture absorption and contamination. Avoid exposure to direct sunlight and extreme temperatures to ensure long-term usability. When handling, use appropriate personal protective equipment such as gloves and safety goggles to minimize risk. It is important to store the compound away from incompatible substances to prevent any chemical reactions. Proper labeling and storage conditions are essential to maintain the integrity of the reagent for laboratory use.
References cited in the TCI brochure
- Motonori Kudou. Prevention of thermal inactivation and aggregation of lysozyme by polyamines European Journal of Biochemistry, 2003. doi:10.1046/j.1432-1033.2003.03850.x
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