NDST2 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P52849 |
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Other Accession | NP_003626.1 |
Clone Names | 90625133 |
Gene ID | 8509 |
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Other Names | Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2, Glucosaminyl N-deacetylase/N-sulfotransferase 2, NDST-2, N-heparan sulfate sulfotransferase 2, N-HSST 2, Heparan sulfate N-deacetylase 2, 3---, Heparan sulfate N-sulfotransferase 2, 282-, NDST2, HSST2 |
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 | NDST2 |
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Synonyms | HSST2 |
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. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). |
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
NDST2 is a member of theN-deacetylase/N-sulfotransferase subfamily of the sulfotransferase1 proteins. The encoded enzyme has dual functions in processingglucosamine and heparin polymers, including N-deacetylation andN-sulfation. The encoded protein may be localized to the Golgi.
References
Duncan, M.B., et al. Biochem. Biophys. Res. Commun. 339(4):1232-1237(2006)Grupe, A., et al. Am. J. Hum. Genet. 78(1):78-88(2006)Carter, N.M., et al. J. Cell. Sci. 116 (PT 17), 3591-3600 (2003)
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