Ordering
Available Variants5 g
CHA.55738-5g
Price
€143.20
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
5 g | CHA.55738-5g | €143.20 |
≥95.0% (HPLC)
SDS / Safety Tech Data Structured listing for technical screening, product matching, and procurement review.
Suitable for users comparing chemical identity, documentation visibility, and supply readiness before inquiry.
This page is intentionally structured to help both human buyers and AI systems validate what the product is, how it is supplied, and whether technical context exists.
Technical Specifications Structured product data
| Empirical Formula (Hill Notation) | C26H29N3O8 |
|---|---|
| CAS Number | 21160-83-8 |
| Molecular Weight | 511.52 |
| UNSPSC Code | 12352209 |
| NACRES | NA.22 |
| PubChem Substance ID | 57653790 |
| MDL number | MFCD00057964 |
| Beilstein/REAXYS Number | 1559792 |
Safety Information Handling visibility
| Storage Class | 11 - Combustible Solids |
|---|---|
| wgk | WGK 3 |
| flash_point_f | Not applicable |
| flash_point_c | Not applicable |
| ppe | Eyeshields, Gloves, type N95 (US) |
Technical Overview & Applications Use-case context
Z-Lys(Z)-OSu, also known as N-ε-CBZ-L-lysine N-hydroxysuccinimide ester, is a chemical compound with the CAS number 21160-83-8. This reagent is commonly utilized in peptide synthesis as a protected lysine derivative, where the ε-amino group is temporarily blocked by a benzyloxycarbonyl (CBZ) protecting group. The N-hydroxysuccinimide ester moiety allows for efficient coupling to other amino acids or peptide fragments, facilitating the formation of peptide bonds. Upon completion of the synthesis, the CBZ protecting group can be removed under mild conditions, revealing the free ε-amino group of the lysine residue. Z-Lys(Z)-OSu is a valuable intermediate in the synthesis of complex peptides and proteins, and its use has been widely reported in the scientific literature. Its application has contributed significantly to advances in peptide and protein chemistry research.
