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anti-Human NDST1 Antibodies:
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Human Monoclonal NDST1 Primary Antibody for IHC (p), ELISA - ABIN561391
Baljinnyam, Iwatsubo, Kurotani, Wang, Ulucan, Iwatsubo, Lagunoff, Ishikawa: Epac increases melanoma cell migration by a heparan sulfate-related mechanism. in American journal of physiology. Cell physiology 2009
Compound heterozygous mutations in NDST1 were identified, in the heparan sulfate N deacetylatase domain of one allele and the sulfotransferase domain of the other allele. This report expands the phenotypic spectrum of Ndst1 deficiency in humans.
Among the genes enriched in this screening, the authors found that TM9SF2 is critical for N-sulfation of heparan sulfate and therefore for chikungunya virus infection because it is involved in the proper localization and stability of NDST1.
Our data confirm NDST1 mutations as a cause of autosomal recessive intellectual disability with a distinctive phenotype, and support an important function of NDST1 in human development.
demonstrate the essential role of domain cooperation within NDST-1 in producing HS with specific domain structures
Upregulation of NDST1 is associated with chemoresistance in breast cancer.
These findings establish NDST1 as a target of miR-24 and demonstrate how such NDST1 suppression in endothelial cells results in reduced responsiveness to VEGFA
MicroRNA-191 targets N-deacetylase/N-sulfotransferase 1 and promotes cell growth in human gastric carcinoma cell line MGC803
Inhibitory peptides of the sulfotransferase domain of the heparan sulfate enzyme, N-deacetylase-N-sulfotransferase-1.
Altered expression of NDST-1 mRNA in glomerular basement membrane in puromycin aminonucleoside nephrosis.
effect of targeted inactivation of the Ndst1 gene on the inflammatory response associated with allergic inflammation
the expression of the NDST-1 isoform was approximately equal at all stages of mast cell maturation
Tubulo-interstitial macrophage influx and fibrosis are reduced by endothelial Ndst1 deficiency in experimental diabetes.
An essential role for Heparin sulfate proteoglycan sulfation via NDST1,2,3 in modulating signal transduction during mouse implantation.
Podocyte-glomerular basement membrane interactions and cytoskeletal organization are disrupted in the glomeruli of the Ndst1-/- mutant mouse model
Although the renal phenotype of the Ndst1(-/-) mouse is mild, the data show that heparan chain N-sulfation plays a key role in podocyte organization.
Targeted ablation of Ndst1 in smooth muscle cells results in altered biomechanical properties of aorta.
Loss of NDST1 causes defective diaphragm vascular development and congenital diaphragmatic hernia.
The results of this study suggested that while Chst14 and its enzymatic products might be of limited importance for neural development, they may contribute to the regeneration-restricting environment in the adult mammalian nervous system
embryonic stem cells lacking both NDST1 and NDST2, expressing a very low sulfated heparan sulfate, can take the initial step toward differentiation into all three germ layers
Deletion of N-deacetylase-N-sulfotransferase1 in smooth muscle did not influence any of the blood pressure parameters measured despite significant decrease in aorta and thoracodorsal artery luminal area.
Lowered expression of NDST1 also results in a higher sulfate content of the heparin synthesized and is accompanied by increased levels of stored MC proteases.
These data provide new evidence that modification of heparan sulfate fine structure through deletion of Ndst1 is sufficient to decrease vascular smooth muscle cell proliferation and alter vascular remodeling.
These findings demonstrate a selective, highly penetrant, cell autonomous effect of Ndst1-mediated sulfation on lobuloalveolar development.
Structural analyses of heparan sulfate produced by stable human embryonic 293 cells expressing mouse NDST-1 mutants indicate that the deacetylase of one enzyme and the sulfotransferase of another can act on the same glucosamine unit.
major changes in the heparan sulfate composition in skeletal muscle tissue derived from NDST-1-/- mice and NDST-/- cultured myotubes.
NDST-1 and C5-epimerase have roles in heparan sulfate structure alterations in mouse tissue
NDST1 and NDST2 have roles in N-sulfation but not in 6-O-sulfation of heparan sulfate
findings show that properly synthesized heparan sulfate is required for the normal development of the brain and face, and that Ndst1 is a modifier of heparan sulfate-dependent growth factor/morphogen signalling in those tissues
analysis of liver NDST1 and NDST2 biosynthesis
results establish an important role of Ndst1 function in FGF signaling during lens development
Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis (By similarity).
, N-HSST 1
, N-heparan sulfate sulfotransferase 1
, [Heparan sulfate]-glucosamine N-sulfotransferase 1
, bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
, glucosaminyl N-deacetylase/N-sulfotransferase 1
, heparan sulfate-N-deacetylase/N-sulfotransferase
, N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1
, N-deacetylase/N-sulfotransferase 1