Phenylthiohydantoin-(Nε-phenylthiocarbamyl)-lysine

≥98%

Reagent Code: #123131
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CAS Number 29635-94-7

science Other reagents with same CAS 29635-94-7

blur_circular Chemical Specifications

scatter_plot Molecular Information
Weight 398.54 g/mol
Formula C₂₀H₂₂N₄OS₂
badge Registry Numbers
MDL Number MFCD00151476
thermostat Physical Properties
Melting Point 162-166°C
inventory_2 Storage & Handling
Storage room temperature

description Product Description

Phenylthiohydantoin-(Nε-phenylthiocarbamyl)-lysine is primarily utilized in the field of protein sequencing and peptide analysis. It serves as a derivative in the Edman degradation process, a method used to determine the amino acid sequence in proteins. By reacting with the N-terminal amino acid of a peptide, it forms a stable phenylthiohydantoin derivative, which can be easily identified through chromatographic techniques. This allows for the sequential removal and identification of amino acids, aiding in the structural analysis of proteins. Additionally, it is employed in biochemical research to study protein modifications and interactions, providing insights into protein function and behavior in various biological systems.

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Test Parameter Specification
Appearance White to Light yellow powder to crystal
Purity (%) 98-100
Infrared Spectrum Conforms to Structure
NMR Conforms to Structure

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Size Availability Unit Price Quantity
inventory 100mg
10-20 days ฿1,395.00

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Phenylthiohydantoin-(Nε-phenylthiocarbamyl)-lysine
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Phenylthiohydantoin-(Nε-phenylthiocarbamyl)-lysine is primarily utilized in the field of protein sequencing and peptide analysis. It serves as a derivative in the Edman degradation process, a method used to determine the amino acid sequence in proteins. By reacting with the N-terminal amino acid of a peptide, it forms a stable phenylthiohydantoin derivative, which can be easily identified through chromatographic techniques. This allows for the sequential removal and identification of amino acids, aiding in the structural analysis of proteins. Additionally, it is employed in biochemical research to study protein modifications and interactions, providing insights into protein function and behavior in various biological systems.
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