99865-70-0

Upstream product

• 174884-11-8 ethyl 4-(4-(hydroxymethyl)phenoxy) butanoate 
• 5084-45-7 6-formyl-2-naphthoic acid 
• 123-08-0 4-hydroxy-benzaldehyde 
• 92991-64-5 ethyl 4-(4-formylphenoxy)butyrate 
• 99842-71-4 4-(4-formylphenoxy)butanitrile 

Downstream Products

• 1622095-16-2 C₂₁H₂₁NO₅ 
• 1622095-12-8 C₂₀H₁₉NO₅ 
• 171674-98-9 C₁₅H₂₀O₄ 
• 1622104-50-0 C₁₅H₂₀O₄ 
• 1622095-42-4 C₂₄H₂₅NO₆ 
• 1622095-41-3 C₂₅H₂₇NO₆ 
• 1622095-06-0 C₁₅H₁₈O₄ 
• 1622095-45-7 C₁₅H₂₀O₄ 
• 1622095-44-6 C₁₄H₁₈O₄ 
• 1622095-43-5 C₁₅H₁₈O₅ 
• 1622095-33-3 C₁₅H₁₈O₄ 
• 1622095-26-4 C₁₅H₂₀O₄ 
• 1622095-24-2 C₁₄H₁₈O₄ 
• 1622095-40-2 C₂₃H₂₃NO₆ 

Relevant academic research and scientific papers

The Development of Highly Fluorescent Hemicyanine and Dicyanoisophorone Dyes for Applications in Dye-Sensitized Solar Cells

Ruthenium-based metal complex dyes have been employed extensively in dye-sensitized solar cells (DSSCs) as photosensitizers, but the cost and toxicity of metal complexes have promoted the development of metal-free organic dyes. The present investigation d

CHEMOSELECTIVE SENSITIVITY BOOSTER FOR TAGGING A PEPTIDE, PEPTIDE CONJUGATE, OR SIMILAR REACTIVE MOLECULE

The invention pertains to chemoselective sensitivity booster for tagging a peptide, peptide conjugate, or similar reactive molecule for analysis of a peptide, protein, antibody, protein bioconjugate, antibody bioconjugate, and similar analytes. The sensitivity booster comprises of sp2 or sp3 nitrogen centers in combination with hydrophobic carbon chains linked with an electrophile or nucleophile for attachment with a peptide, peptide conjugate, or molecules with similar reactivity.

Sensitivity booster for mass detection enables unambiguous analysis of peptides, proteins, antibodies, and protein bioconjugates

A chemical tag enhances peptide detection by multiple orders in mass spectrometry. The substantial improvement in the peptide mapping along with simplified and enhanced fragmentation pattern enables the unambiguous sequencing of a protein and antibody. The chemoselective sensitivity booster provides a tool for remarkably improved analysis of protein bioconjugates.

Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology

Chemical biology research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chemical technology. Here, we report a chemical platform that enables site-selective labeling of native proteins. Initially, a reversible intermolecular reaction places the "chemical linchpins" globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiological conditions and capacitates the late-stage installation of various tags. The chemical platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of additional chromatography tag. The methodology allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymatic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 positive SKBR-3 breast cancer cells.

Aldehydes can switch the chemoselectivity of electrophiles in protein labeling

We show that the chemoselectivity of an electrophile in protein labeling can be promiscuous. An aldehyde enables switching of chemoselectivity of an epoxide and a sulfonate ester along with an enhanced rate of reaction. The chemical technology renders single-site installation of diverse probes on a protein and delivers analytically pure tagged proteins.

Single-site labeling of lysine in proteins through a metal-free multicomponent approach

We report a chemoselective and site-selective approach that distinguishes one Lys from its multiple copies, N-terminus, and other competitors. The phospha-Mannich protocol works with multiple proteins and installs probes without structural and functional

Synthesis and absolute configurations of six natural phenylpropanoids

In an effort to find answers to the tantalizing questions about the absolute configurations of a group of long-known natural phenylpropanoids with very similar structures but different signs for the optical rotations, the compounds in question were synthe

PHARMACEUTICAL PREPARATIONS COMPRISING INSULIN, ZINC IONS AND A ZINC-BINDING LIGAND

Novel preparations comprising branched ligands for the HisB10 Zn2+ sites of the R-state insulin hexamer. The preparations have a prolonged action designed for flexible injection regimes.

PHAMACEUTICAL PREPARATIONS COMPRISING INSULIN

Novel preparations comprising ligands for the HisB10 Zn2+ sites of the R-state insulin hexamer wherein the ligand is extended by protamine that are capable of prolonging the ac-tion of insulin preparations.

Stabilised insulin compositions

The present invention provides pharmaceutical compositions comprising insulin and novel ligands for the HisB10 Zn2+ sites of the R-state insulin hexamer. The resulting preparations have improved physical and chemical stability.