3 Results for "

N-acetyl modification

" in MedChemExpress (MCE) Product Catalog:
Products (3)

3 Results for "N-acetyl modification" in MCE Product Catalog:

Cat. No.: HY-134222A
CAS No.: 16354-58-8
Purity:  ≥98.0%
Synonyms: N-acetyl-L-serine
N-Acetylserine (N-Acetyl-L-serine) is a complement pathway modulator targeting activated third complement protein (C3b) and an amino-terminal residue (an N-terminal acetylation modification group). N-Acetylserine reacts with the exposed thioester group of C3b via its hydroxyl group, thereby blocking the covalent binding of glycerol to this thioester group. N-Acetylserine widely exists in soluble proteins of mammalian cells (accounting for approximately 80% of such proteins). N-Acetylserine has a blocking property that prevents direct Edman sequencing of proteins; deblocking is achievable through trifluoroacetic acid-catalyzed N→O acetyl migration followed by β-elimination. N-Acetylserine is suitable for sequencing of proteins with N-terminal acetylserine modification .
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Cat. No.: HY-148596
CAS No.: 528-04-1
Synonyms: UDP-N-acetyl-D-glucosamine; Uridine diphospho-N-acetylglucosamine; UDP-N-acetylglucosamine
UDP-GlcNAc (UDP-N-Acetyl-D-glucosamine) is an important component and precursor of bacterial peptidoglycan. UDP-GlcNAc is a nucleotide sugar used by Glycosyltransferases to synthesize glycoproteins, glycosaminoglycans, glycolipids, and glycoRNA. UDP-GlcNAc also serves as the donor substrate for forming O-GlcNAc, a dynamic intracellular protein modification involved in diverse signaling and disease processes. UDP-GlcNAc is the sugar nucleotide donor for the synthesis of O-GlcNAc modified proteins. UDP-GlcNAc also acts as a full agonist of the P2Y14 receptor and inhibits the formation of cAMP. UDP-GlcNAc can be used in studies related to bacterial infections .
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Cat. No.: HY-185452
CAS No.: 28070-54-4
Target:  

Drug Intermediate

Research Areas:  

Others

N4-Acetyldeoxycytidine triphosphate is a terminal deoxynucleotidyl transferase substrate. N4-Acetyldeoxycytidine triphosphate acts as a substrate for calf thymus terminal deoxynucleotidyl transferase and undergoes polymerization to form extended polydeoxynucleotide chains .
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