Z-LYS-SBZL HCL

Reagent Code: #73432
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CAS Number 69861-89-8

science Other reagents with same CAS 69861-89-8

blur_circular Chemical Specifications

scatter_plot Molecular Information
Weight 422.97 g/mol
Formula C₂₁H₂₇ClN₂O₃S
badge Registry Numbers
MDL Number MFCD00058089
inventory_2 Storage & Handling
Storage -20 °C, sealed, dry

description Product Description

Z-LYS-SBZL HCl is primarily used in peptide synthesis as a protecting group for lysine residues. Its application is crucial in preventing unwanted side reactions during the formation of peptide bonds, ensuring the synthesis proceeds efficiently. This compound is particularly valuable in the production of complex peptides and proteins, where selective protection and deprotection of amino acids are necessary. Additionally, it finds use in biochemical research for studying enzyme-substrate interactions and protein folding, as it allows for precise control over the chemical environment of lysine residues. Its stability and ease of removal make it a preferred choice in both industrial and academic settings for advanced peptide chemistry.

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Test Parameter Specification
Appearance White powder
Infrared Spectrum Conforms to Structure
NMR Conforms to Structure

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Size Availability Unit Price Quantity
inventory 100mg
10-20 days ฿15,680.00
inventory 25mg
10-20 days ฿6,480.00

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Z-LYS-SBZL HCL
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Z-LYS-SBZL HCl is primarily used in peptide synthesis as a protecting group for lysine residues. Its application is crucial in preventing unwanted side reactions during the formation of peptide bonds, ensuring the synthesis proceeds efficiently. This compound is particularly valuable in the production of complex peptides and proteins, where selective protection and deprotection of amino acids are necessary. Additionally, it finds use in biochemical research for studying enzyme-substrate interactions and

Z-LYS-SBZL HCl is primarily used in peptide synthesis as a protecting group for lysine residues. Its application is crucial in preventing unwanted side reactions during the formation of peptide bonds, ensuring the synthesis proceeds efficiently. This compound is particularly valuable in the production of complex peptides and proteins, where selective protection and deprotection of amino acids are necessary. Additionally, it finds use in biochemical research for studying enzyme-substrate interactions and protein folding, as it allows for precise control over the chemical environment of lysine residues. Its stability and ease of removal make it a preferred choice in both industrial and academic settings for advanced peptide chemistry.

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