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Mouse Anti-NDST1 Recombinant Antibody (CBWJN-0076) (CBMAB-N1591-WJ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBWJN-0076
Antibody Isotype
IgG2a, κ
Application
ELISA, IHC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1
Introduction
This gene encodes a member of the heparan sulfate/heparin GlcNAc N-deacetylase/ N-sulfotransferase family. The encoded enzyme is a type II transmembrane protein that resides in the Golgi apparatus. The encoded protein catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to nitrogen of glucosamine in heparan sulfate. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]
Entrez Gene ID
3340
UniProt ID
P52848
Alternative Names
N-Deacetylase And N-Sulfotransferase 1; [Heparan Sulfate]-Glucosamine N-Sulfotransferase 1; Heparan Sulfate/Heparin GlcNAc N-Deacetylase/GlcN N-Sulfotransferase 1; N-Deacetylase/N-Sulfotransferase (Heparan Glucosaminyl) 1; Glucosaminyl N-Deacetylase/N-Sulfotransferase 1; N-Heparan Sulfate Sulfotransferase 1; N-Deacetylase-N-Sulfotransferase 1; N-HSST 1; HSNST 1; NDST-1;
Function
Isoform 1:
Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate (PubMed:9230113, PubMed:9744796, PubMed:35137078).

Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis (PubMed:9230113).

Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response (By similarity).

Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).

Isoform 3:
Lacks both N-deacetylase and N-sulfotransferase activities. Acts as a dominant negative on isoform 1, likely by changing the composition of enzyme complexes responsible for elongation and modification of heparan sulfates.
Biological Process
Aorta development Source: Ensembl
Cardiac septum development Source: Ensembl
Cell population proliferation Source: Ensembl
Coronary vasculature development Source: Ensembl
Embryonic neurocranium morphogenesis Source: Ensembl
Embryonic viscerocranium morphogenesis Source: Ensembl
Fibroblast growth factor receptor signaling pathway Source: Ensembl
Forebrain development Source: Ensembl
Glycosaminoglycan biosynthetic process Source: Reactome
Heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: UniProtKB
Heparin biosynthetic process Source: UniProtKB-UniPathway
Inflammatory response Source: UniProtKB-KW
Midbrain development Source: Ensembl
Positive regulation of MAPK cascade Source: Ensembl
Positive regulation of smoothened signaling pathway Source: Ensembl
Protein sulfation Source: Ensembl
Respiratory gaseous exchange by respiratory system Source: Ensembl
Cellular Location
Isoform 1:
Golgi apparatus
trans-Golgi network membrane
cis-Golgi network membrane
Isoform 3:
Golgi apparatus
cis-Golgi network membrane
Involvement in disease
Mental retardation, autosomal recessive 46 (MRT46):
A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT46 manifestations include delayed psychomotor development apparent from infancy or early childhood, delayed or absent expressive speech, hypotonia, and therapy-responsive seizures in some patients. Behavioral abnormalities are variable and include aggression, self-injurious behavior, and sleep disturbances.
Topology
Cytoplasmic: 1-17
Helical: 18-39
Lumenal: 40-882
More Infomation

Suzuki, M., Takada, S., & Mii, Y. (2024). Dissection of N‐deacetylase and N‐sulfotransferase activities of NDST1 and their effects on Wnt8 distribution and signaling in Xenopus embryos. Development, Growth & Differentiation.

Aguilar-Calvo, P., Malik, A., Sandoval, D. R., Barback, C., Orrù, C. D., Standke, H. G., ... & Sigurdson, C. J. (2023). Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection. PLoS Pathogens, 19(9), e1011487.

Khosrowabadi, E., Mignon-Ravix, C., Riccardi, F., Cacciagli, P., Desnous, B., Sigaudy, S., ... & Molinari, F. (2023). Loss of NDST1 N-sulfotransferase activity is associated with autosomal recessive intellectual disability. Human Molecular Genetics, ddad203.

Yamamoto, T., Kambayashi, Y., Tsukano, K., & Michiue, T. (2023). Ndst1, a heparan sulfate modification enzyme, regulates neuroectodermal patterning by enhancing Wnt signaling in Xenopus. Development, Growth & Differentiation, 65(3), 153-160.

Missaghian, P., Dierker, T., Khosrowabadi, E., Axling, F., Eriksson, I., Ghanem, A., ... & Kjellén, L. (2022). A dominant negative splice variant of the heparan sulfate biosynthesis enzyme NDST1 reduces heparan sulfate sulfation. Glycobiology, 32(6), 518-528.

Otsuka, T., Kan, H. M., Mason, T. D., Nair, L. S., & Laurencin, C. T. (2022). Overexpression of NDST1 attenuates fibrotic response in murine adipose-derived stem cells. Stem Cells and Development, 31(23-24), 787-798.

Khan, A., Miao, Z., Umair, M., Ullah, A., Alshabeeb, M. A., Bilal, M., ... & Carapito, R. (2020). Two Cases of recessive intellectual disability caused by NDST1 and METTL23 variants. Genes, 11(9), 1021.

Xue, J., Yang, M., Hua, L. H., & Wang, Z. P. (2019). MiRNA-191 functions as an oncogene in primary glioblastoma by directly targeting NDST1. European Review for Medical & Pharmacological Sciences, 23(14).

Mo, X. B., Lei, S. F., Zhang, Y. H., & Zhang, H. (2019). Integrative analysis identified IRF6 and NDST1 as potential causal genes for ischemic stroke. Frontiers in Neurology, 10, 517.

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For research use only. Not intended for any clinical use.

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