Need Assistance?

US & Canada:
+
UK: +

FAQs

Resources

Our Highlights

GMP Grade Efficient workshop for GMP production.
Optimal Prices Buying products on this site guarantees the best price!
Commercial Batches Independent GMP manufacturing suites that handle commercial batches
Prompt Delivery Warehouses in multiple cities to ensure timely delivery
Flexible Quantity Quantities available from milligrams to ton

Application Area

Nα-Boc-Nω,Nω'-bis-Z-L-arginine N-hydroxysuccinimide ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

BOC-Amino Acids

Catalog number

BAT-004301

CAS number

76052-29-4

Molecular Formula

C31H37N5O10

Molecular Weight

639.60

Nα-Boc-Nω,Nω'-bis-Z-L-arginine N-hydroxysuccinimide ester

IUPAC Name

(2,5-dioxopyrrolidin-1-yl) (2S)-5-[bis(phenylmethoxycarbonylamino)methylideneamino]-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoate

Synonyms

Boc-L-Arg(Z)2-Osu; (2,5-dioxopyrrolidin-1-yl) (2S)-5-[bis(phenylmethoxycarbonylamino)methylideneamino]-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoate

Appearance

White powder

Purity

99%

Density

1.31±0.1 g/cm3(Predicted)

Storage

Store at 2-8 °C

InChI

InChI=1S/C31H37N5O10/c1-31(2,3)45-30(42)33-23(26(39)46-36-24(37)16-17-25(36)38)15-10-18-32-27(34-28(40)43-19-21-11-6-4-7-12-21)35-29(41)44-20-22-13-8-5-9-14-22/h4-9,11-14,23H,10,15-20H2,1-3H3,(H,33,42)(H2,32,34,35,40,41)/t23-/m0/s1

InChI Key

HAKDQDAGZLXYNM-QHCPKHFHSA-N

Canonical SMILES

CC(C)(C)OC(=O)NC(CCCN=C(NC(=O)OCC1=CC=CC=C1)NC(=O)OCC2=CC=CC=C2)C(=O)ON3C(=O)CCC3=O

Nα-Boc-Nω,Nω'-bis-Z-L-arginine N-hydroxysuccinimide ester, a specialized reagent in peptide synthesis and biochemical research, boasts diverse applications. Here are the key applications highlighted with high perplexity and burstiness:

Peptide Synthesis: Widely employed in peptide synthesis, Nα-Boc-Nω,Nω'-bis-Z-L-arginine N-hydroxysuccinimide ester plays a pivotal role in enhancing the coupling of amino acid residues. Its exceptional reactivity and selectivity mitigate the occurrence of unwanted side reactions, ensuring the efficient assembly of intricate peptide sequences essential for both research and therapeutic advancements.

Bioconjugation: Indispensable in bioconjugation techniques, this compound serves as a vital link between proteins, peptides, and other biomolecules with diverse substrates. Its active ester group readily reacts with primary amines, forming stable amide bonds. This versatility positions it as a premier reagent for developing bioconjugates utilized in diagnostics, drug delivery systems, and imaging applications, pioneering advancements in biotechnology.

Proteomics Research: Within the realm of proteomics, Nα-Boc-Nω,Nω'-bis-Z-L-arginine N-hydroxysuccinimide ester plays a crucial role in modifying peptides and proteins for mass spectrometry analysis. Tagging proteins or peptides enhances the accuracy and sensitivity of analysis, facilitating precise protein identification and deeper exploration into protein interactions and functions, enriching our understanding of cellular processes.

Drug Development: In the realm of drug development, this compound emerges as a linchpin in the creation of peptide-based therapeutics. Its targeted modification of drug candidates enhances stability, efficacy, and specificity of peptide drugs, unlocking new horizons in therapeutic interventions. Leveraging this ester in drug synthesis promises novel treatments for diverse ailments, including cancer and autoimmune disorders, propelling the frontier of pharmaceutical innovation.

1. Selective protein N-terminal labeling with N-hydroxysuccinimide esters

Hanjie Jiang, Gabriel D D'Agostino, Philip A Cole, Daniel R Dempsey Methods Enzymol. 2020;639:333-353. doi: 10.1016/bs.mie.2020.04.018. Epub 2020 Apr 28.

In order to gain detailed insight into the biochemical behavior of proteins, researchers have developed chemical tools to incorporate new functionality into proteins beyond the canonical 20 amino acids. Important considerations regarding effective chemical modification of proteins include chemoselectivity, near stoichiometric labeling, and reaction conditions that maintain protein stability. Taking these factors into account, we discuss an N-terminal labeling strategy that employs a simple two-step "one-pot" method using N-hydroxysuccinimide (NHS) esters. The first step converts a R-NHS ester into a more chemoselective R-thioester. The second step reacts the in situ generated R-thioester with a protein that harbors an N-terminal cysteine to generate a new amide bond. This labeling reaction is selective for the N-terminus with high stoichiometry. Herein, we provide a detailed description of this method and further highlight its utility with a large protein (>100kDa) and labeling with a commonly used cyanine dye.

2. General protein-protein cross-linking

Alice Alegria-Schaffer Methods Enzymol. 2014;539:81-7. doi: 10.1016/B978-0-12-420120-0.00006-2.

This protocol describes a general protein-to-protein cross-linking procedure using the water-soluble amine-reactive homobifunctional BS(3) (bis[sulfosuccinimidyl] suberate); however, the protocol can be easily adapted using other cross-linkers of similar properties. BS(3) is composed of two sulfo-NHS ester groups and an 11.4 Å linker. Sulfo-NHS ester groups react with primary amines in slightly alkaline conditions (pH 7.2-8.5) and yield stable amide bonds. The reaction releases N-hydroxysuccinimide (see an application of NHS esters on Labeling a protein with fluorophores using NHS ester derivitization).

3. Amine coupling through EDC/NHS: a practical approach

Marcel J E Fischer Methods Mol Biol. 2010;627:55-73. doi: 10.1007/978-1-60761-670-2_3.

Surface plasmon resonance (SPR) is one of the leading tools in biomedical research. The challenge in its use is the controlled positioning of one of the components of an interaction on a carefully designed surface. Many attempts in interaction analysis fail due to the non-functional or unsuccessful immobilization of a reactant onto the complex matrix of that surface. The most common technique for linking ligands covalently to a hydrophilic solid surface is amine coupling via reactive esters. In this chapter detailed methods and problem discussions will be given to assist in fast decision analysis to optimize immobilization and regeneration. Topics in focus are different coupling techniques for small and large molecules, streptavidin-biotin sandwich immobilization, and optimizing regeneration conditions.