108320-87-2 Usage
Description
Udp-alpha-d-n-acetylgalactosamine, disodium salt is a donor substrate for N-acetylgalactosaminyltransferases. Udp-alpha-d-n-acetylgalactosamine, disodium salt is useful in the synthesis of aryl azide derivatives that can be employed in affinity labeling of glycosyltransferases and UDP-HexNAc pyrophosphorylase. Udp-alpha-d-n-acetylgalactosamine, disodium salt can be used to treat and prevent renal inflammation association with infection.
Chemical Properties
White to off-white crystalline powder
Uses
Different sources of media describe the Uses of 108320-87-2 differently. You can refer to the following data:
1. Uridine 5′-Diphospho-N-acetylgalactosamine Disodium Salt can be used to treat and prevent renal inflammation association with infection.
2. Uridine 5′-diphospho-N-acetylgalactosamine disodium salt has been used as a substrate for polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-T).
General Description
Uridine diphosphate (UDP)-GalNAc acts as a precursor in the biosynthesis of O-linked oligosaccharide. It also acts as a substrate for synthesis of chitin, a vital element of cell walls in fungi and of exoskeletons of arthropods and insects.
Check Digit Verification of cas no
The CAS Registry Mumber 108320-87-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,8,3,2 and 0 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 108320-87:
(8*1)+(7*0)+(6*8)+(5*3)+(4*2)+(3*0)+(2*8)+(1*7)=102
102 % 10 = 2
So 108320-87-2 is a valid CAS Registry Number.
108320-87-2Relevant articles and documents
Chemoenzymatic synthesis of uridine diphosphate-GlcNAc and uridine diphosphate-GalNAc analogs for the preparation of unnatural glycosaminoglycans
Masuko, Sayaka,Bera, Smritilekha,Green, Dixy E.,Weiwer, Michel,Liu, Jian,Deangelis, Paul L.,Linhardt, Robert J.
experimental part, p. 1449 - 1456 (2012/03/11)
Eight N-acetylglucosamine-1-phosphate and N-acetylgalactosamine-1-phosphate analogs have been synthesized chemically and were tested for their recognition by the GlmU uridyltransferase enzyme. Among these, only substrates that have an amide linkage to the C-2 nitrogen were transferred by GlmU to afford their corresponding uridine diphosphate(UDP)-sugar nucleotides. Resin-immobilized GlmU showed comparable activity to nonimmobilized GlmU and provides a more facile final step in the synthesis of an unnatural UDP-donor. The synthesized unnatural UDP-donors were tested for their activity as substrates for glycosyltransferases in the preparation of unnatural glycosaminoglycans in vitro. A subset of these analogs was useful as donors, increasing the synthetic repertoire for these medically important polysaccharides.
