NDST4 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9H3R1 |
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Clone Names | 110811140 |
Gene ID | 64579 |
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Other Names | Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4, Glucosaminyl N-deacetylase/N-sulfotransferase 4, NDST-4, N-heparan sulfate sulfotransferase 4, N-HSST 4, Heparan sulfate N-deacetylase 4, 3---, Heparan sulfate N-sulfotransferase 4, 282-, NDST4, HSST4 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | NDST4 |
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Synonyms | HSST4 |
Function | 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 disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity (By similarity). |
Cellular Location | Golgi apparatus membrane; Single- pass type II membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. Has low deacetylase activity but high sulfotransferase activity (By similarity).
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Kalsi, G., et al. Hum. Mol. Genet. 19(12):2497-2506(2010)Treutlein, J., et al. Arch. Gen. Psychiatry 66(7):773-784(2009)Aikawa, J., et al. J. Biol. Chem. 276(8):5876-5882(2001)
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