Putrescine Dihydrochloride [for Protein Research] TCI P3082

Chemical Identity

CAS No.: 333-93-7
Purity: >98.0%(T)

Rp 848.400,00

~~Rp 593.250,00~~ Rp 848.400,00

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Berat 5g 25g

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Putrescine Dihydrochloride (TCI P3082), with CAS number 333-93-7, is a chemical compound widely used in life science research, particularly in protein studies and biomolecule stabilization. It plays a crucial role in laboratories where researchers are involved in modifying proteins or adjusting molecular structures. This compound is essential for experiments that require specific chemical interactions, making it a reliable and commonly used reagent in biochemical applications. Its stability and availability make it a go-to choice for scientists working in various fields of molecular biology and biochemistry.

Putrescine Dihydrochloride is valued for its chemical properties that enable effective interaction with proteins. It has a unique structure that allows it to bind metal ions and form complexes with protein molecules. These characteristics make it ideal for applications that involve protein modification or reaction environment control. Its ability to stabilize biomolecules under specific conditions enhances its utility in both basic and applied research. As a result, it is a preferred choice for researchers looking to manipulate or study protein behavior in controlled settings.

In Indonesian laboratories, Putrescine Dihydrochloride is commonly used in life science research, especially in protein studies and biomedical applications. Its role in stabilizing biomolecules and supporting protein modification makes it an essential component in many experimental setups. Researchers in Indonesia rely on this compound for its consistent performance and compatibility with various biochemical protocols, ensuring reliable results in their studies.

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

Related TCI products

Protein modification experiments benefit from Putrescine Dihydrochloride due to its ability to interact with and stabilize protein structures.
Biomolecule stabilization is enhanced by its chemical properties, making it suitable for preserving molecular integrity during experiments.
Metal ion binding applications utilize its structure to form complexes, aiding in the study of metal-dependent biochemical processes.
Reaction environment control is supported by its stability, allowing researchers to maintain consistent conditions for protein studies.
Biomedical research applications leverage its role in modulating protein behavior, contributing to drug development and therapeutic studies.

From the TCI brochure

Preventing aggregation of target proteins
Protein stabilization

Brand	TCI
CAS number	333-93-7
Molecular formula	—
Purity	—
Category	Life Science > Biochemicals and Reagents > Stabilization of Biomolecules
Pack sizes	Available in various quantities as per standard laboratory reagent packaging
Physical form	Solid powder
Storage	Store in a cool, dry place away from direct light and moisture

Putrescine Dihydrochloride should be stored in a cool, dry environment to maintain its chemical stability and prevent degradation. It is recommended to keep the compound in airtight containers to avoid moisture exposure, which could affect its performance in experiments. Laboratory personnel should handle the material with care, using appropriate personal protective equipment such as gloves and safety goggles to ensure safety. It is important to store it away from incompatible substances to prevent any chemical reactions. Regular checks of storage conditions should be conducted to ensure the compound remains in optimal condition for use in research applications. Proper labeling of containers is also essential to prevent accidental misuse or contamination.

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