N-Acetyl-D-galactosamine 6-sulfate (GalNAc-6S) is used as a substrate to identify, differentiate and characterize N-acetylgalactosamine sulfatase(s). GalNAc-6S is used to study the rare autosomal recessive disorder Mucopolysaccharidosis IVA (MPS IVA).
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Bottomless glass bottle. Contents are inside inserted fused cone.
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Current pharmaceutical biotechnology, 12(6), 931-945 (2011-04-22)
Mucopolysaccharidosis IVA (MPS IVA), also known as Morquio A, is a rare, autosomal recessive disorder caused by a deficiency of the lysosomal enzyme N-acetylgalatosamine-6-sulfate-sulfatase (GALNS), which catalyzes a step in the catabolism of glycosaminoglycans (GAGs), keratan sulfate (KS) and chondroitin-6-sulfate
The Biochemical journal, 248(3), 755-764 (1987-12-15)
Initial purification of N-acetylgalactosamine-4-sulphate sulphatase from human liver homogenates containing approx. 1 mg of enzyme in 26 g of soluble proteins was achieved by a six-column chromatography procedure and yielded approx. 40 micrograms of a single major protein species. Enzyme
Mucopolysaccharidosis type IVA or Morquio A syndrome is characterized by the lack of N-acetylgalactosamine-6-sulfate-sulfatase and the accumulation of keratan sulfate and chondroitin-6-sulfate in the lysosomes. At least, 148 mutations and 16 polymorphisms were identified in the GALNS gene.The aim of
Physical chemistry chemical physics : PCCP, 21(14), 7367-7377 (2019-03-23)
Glycosaminoglycans are linear carbohydrate polymers with essential roles in many biological processes. Chondroitin sulfate (CS) is one of them, omnipresent in living organisms as an important structural component of cartilage. It provides much of its resistance to compression. Despite its
The Biochemical journal, 279 ( Pt 2), 515-520 (1991-10-15)
Human N-acetylgalactosamine 6-sulphatase (EC 3.1.6.14), which is involved in the lysosomal degradation of the glycosaminoglycans keratan sulphate and chondroitin 6-sulphate, was purified more than 130,000-fold in 2.8% yield from liver by an eight-step column procedure. One major form was identified
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