Recombinant Human Bifunctional Heparan Sulfate N-Deacetylase/N-Sulfotransferase 1 (NDST1) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-03084P

Greater than 90% as determined by SDS-PAGE.
Recombinant Human Bifunctional Heparan Sulfate N-Deacetylase/N-Sulfotransferase 1 (NDST1) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-03084P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Bifunctional Heparan Sulfate N-Deacetylase/N-Sulfotransferase 1 (NDST1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P52848 |
Target Symbol | NDST1 |
Synonyms | NDST1; HSST; HSST1; Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1; EC 2.8.2.8; Glucosaminyl N-deacetylase/N-sulfotransferase 1; NDST-1; N-heparan sulfate sulfotransferase 1; N-HSST 1; [Heparan sulfate]-glucosamine N-sulfotransferase 1; HSNST 1) [Includes: Heparan sulfate N-deacetylase 1; EC 3.-.-.-); Heparan sulfate N-sulfotransferase 1; EC 2.8.2.-)] |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | GWKRGLEPSADAPEPDCGDPPPVAPSRLLPLKPVQAATPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDDIFVGKEGTRMKVEDVKALFDTQNELRAHIPNFTFNLGYSGKFFHTGTNAEDAGDDLLLSYVKEFWWFPHMWSHMQPHLFHNQSVLAEQMALNKKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQVWSIRVTSTEEYPHLKPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSSELDKIINGGELFLTVLLNPVSAPQPMAAGEKGLLHSLSAADTGFLEPGKGGEA |
Expression Range | 40-556aa |
Protein Length | Partial of Isoform 2 |
Mol. Weight | 73.5kDa |
Research Area | Immunology |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target 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. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response. Required for the exosomal release of SDCBP, CD63 and syndecan. |
Subcellular Location | Golgi apparatus membrane; Single-pass type II membrane protein. |
Protein Families | Sulfotransferase 1 family, NDST subfamily |
Database References | HGNC: 7680 OMIM: 600853 KEGG: hsa:3340 STRING: 9606.ENSP00000261797 UniGene: PMID: 28211985 |