TCI A3530 1119-34-2 H-Arg-OH.HCl is a chemical compound widely used in protein research within laboratory settings. This compound, known as N-hydroxyarginine hydrochloride, serves as a key reagent in biochemical experiments, particularly in the study of protein structures and functions. It is commonly utilized in the synthesis of peptides and proteins, as well as in the modification of amino acid side chains. Its role in laboratory research is critical for understanding molecular interactions and biological processes.
The compound’s chemical properties make it a preferred choice for researchers. It exhibits good solubility in both organic solvents and water, which simplifies its use in various experimental protocols. Additionally, its stability under normal laboratory conditions ensures consistent results across multiple experiments. The ability of H-Arg-OH.HCl to bind with proteins and act as an ion chelator further enhances its utility in biochemical applications. These characteristics make it a reliable and versatile reagent in both academic and industrial research.
In Indonesian laboratories, TCI A3530 1119-34-2 H-Arg-OH.HCl is frequently used in studies related to chronic diseases such as diabetes and cardiovascular conditions. It is also employed in the development of pharmaceuticals and diagnostic tools. Due to its effectiveness and reliability, it is considered an essential component in high-level research laboratories across Indonesia.
Advantages (TCI brochure)
- Arginine is widely used as an additive for protein refolding
- Amino acid derivatives with charged side chains are useful for inhibiting protein aggregation
- 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
- TCI A3531 26340-89-6 H-Arg-OMe.2HCl [for Protein Research]
- TCI A0806 14620-72-5 Dimethyl Adipimidate Dihydrochloride [Cross-linking Agent for Protein Research]
- TCI S0834 3810-74-0 Streptomycin Sulfate [for Protein Research]
- TCI S0246 34490-86-3 Dimethyl Suberimidate Dihydrochloride [Cross-linking Agent for Protein Research]
- TCI P3082 333-93-7 Putrescine Dihydrochloride [for Protein Research]
- TCI P2957 259244-14-9 Spermidine Phosphate [for Protein Research]
- Protein synthesis and modification experiments benefit from its role in amino acid side chain interactions and peptide bond formation.
- Biochemical assays require its ability to bind with proteins and act as an ion chelator, enhancing the accuracy of analytical results.
- Diagnostic tool development utilizes its solubility and reactivity in creating stable and reliable test reagents.
- Pharmaceutical research employs it in the design of drug molecules that target specific protein pathways.
- Chronic disease studies leverage its role in understanding molecular mechanisms related to metabolic and cardiovascular disorders.
From the TCI brochure
- Protein refolding
- Preventing aggregation of target proteins
| Brand | TCI |
|---|---|
| CAS number | 1119-34-2 |
| Molecular formula | — |
| Purity | — |
| Category | TCI |
| Pack sizes | — |
| Physical form | — |
| Storage | Store in a cool, dry place away from direct light |
This compound should be stored in a cool, dry environment, away from direct sunlight and moisture. It is recommended to use airtight containers to prevent exposure to humidity, which may affect its stability. Due to its chemical nature, it should be handled with appropriate personal protective equipment, such as gloves and safety goggles, to ensure laboratory safety. While it is not classified as hazardous under standard conditions, proper ventilation should be maintained during use. The compound is non-toxic and easy to handle, making it suitable for routine laboratory use. Always follow standard laboratory safety protocols when working with chemical reagents to ensure a safe and controlled environment.
References cited in the TCI brochure
- K. Shiraki. Biophysical Effect of Amino Acids on the Prevention of Protein Aggregation Journal of Biochemistry, 2002. doi:10.1093/oxfordjournals.jbchem.a003261
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