Techniques for detecting, quantifying and localizing antigens and antibodies — ELISA, Western blotting, immunohistochemistry and flow cytometry. Below are the protocols, FAQs and technical articles in our knowledge base tagged with this topic.
In 2026, Roy and Mandal published a study in RSC Advances titled “New benzotriazole–sulfonate coupling reagents and applications,” reporting a class of benzotriazole–sulfonate coupling reagents. Among them, CTSOBt, namely O-benzotriazolyl 5-chlorothiophene-2-sulfonate and recorded in the ...
In peptide synthesis, impurities do not always originate from “incomplete coupling” or “incomplete deprotection.” Many quality issues arise because certain functional groups enter undesired reaction pathways under specific conditions. Carboxyl and hydroxyl groups are two typical ...
The challenges in peptide synthesis often lie not only in whether peptide bonds can be formed, but also in whether the intermediates after each reaction step can dissolve, be separated, and continue to undergo subsequent transformations. For some peptides with high hydrophobicity, long ...
Abnormal impurities in peptide synthesis are usually not caused by a single factor. Instead, they often result from the combined effects of sequence characteristics, protecting-group strategy, reagent condition, washing efficiency, and post-treatment conditions. In solid-phase peptide synthesis ...
The core issue in peptide synthesis is no longer simply “what methods are available to link amino acids together,” but rather how to choose a more suitable preparation route for peptides of different lengths, sequence characteristics, modification requirements, and scale-up goals, while ...
In peptide synthesis, what is often truly difficult to control is not whether an amide bond can be formed, but rather how to minimize epimerization at the α-stereogenic center of the activated carboxylic acid component during activation and the subsequent bond-forming process. This issue is ...
What is commonly described as “low racemization” in peptide synthesis is, in essence, the effort to minimize loss of configuration at the amino acid stereocenter during bond formation, especially at the α-position of the activated carboxylic acid component. Recent reviews have repeatedly ...
“Racemization” in peptide synthesis is often discussed as if it were mainly a question of whether one coupling reagent is better than another. From the standpoint of reaction chemistry, however, what deserves greater caution is the period after the carboxylic acid has been activated. In many ...
The full name of Boc-Oxyma is ethyl 2-(tert-butoxycarbonyloxyimino)-2-cyanoacetate, i.e., 2-(tert-butoxycarbonyloxyimino)-2-cyanoacetic acid ethyl ester. Based on the currently available published literature, Boc-Oxyma has developed three main lines of application together with one bridging use ...
In amide and peptide synthesis, whether a bond can be formed is certainly important. However, for amino acids, peptide fragments, and chiral carboxylic acid substrates containing an α-stereogenic center, another issue often plays an equally decisive role in determining the quality of the ...
Peptide synthesis is not a new problem. Since Merrifield established solid-phase peptide synthesis, resin supports, protecting-group strategies, coupling reagents, and heating methods have continued to evolve, with the same fundamental goals: improving chain-extension efficiency, reducing side ...
Peptide synthesis has long been organized around the basic sequence of protection–coupling–deprotection. Traditional routes are mature and reliable and, when combined with solid-phase synthesis and liquid-phase fragment assembly, already support the research and preparation of many peptide ...
In peptide synthesis, Boc protection groups are widely used to protect the amino terminus of amino acids to prevent unnecessary reactions during synthesis. After the peptide synthesis is complete, the peptide is released from the resin through the cleavage and deprotection steps, and these ...
Solid-phase peptide synthesis (SPPS) is a revolutionary biochemical technique that has become the primary method for synthesizing peptides and proteins since its introduction in the 1960s. Robert Bruce Merrifield first proposed the concept of SPPS in 1963, and this groundbreaking work not only ...
Techniques often explored alongside immunological experiments.
