Recombinant Human HS2ST1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6335-ST

R&D Systems, part of Bio-Techne
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6335-ST-020
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Key Product Details

Source

CHO

Accession #

Q7LGA3

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1 protein
Met59-Asn356, with an N-terminal 6-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His

Predicted Molecular Mass

36 kDa

SDS-PAGE

38-40 kDa, reducing conditions

Activity

Measured by its ability to transfer sulfate from PAPS to heparan sulfate.
The specific activity is >75 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

6335-ST
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1

Heparan sulfate is a highly sulfated polysaccharide found on the cell surface and within the extracellular matrix. Typically, it is covalently attached to the protein core of proteoglycans, such as syndecans and glypicans. Heparin, on the other hand, can be considered as a highly sulfated version of heparan sulfate that is predominantly found in mast cells. Both heparin and heparan sulfate contain disaccharide repeats of uronic acid and N‑acetylglucosamine and are modified by the same sulfotransferases (1, 2). The uronic acid residues are either glucuronic acid or iduronic acid and maybe sulfated at the 2-O position by heparan sulfate 2‑O sulfotransferase 1 (HS2ST1) (3, 4). HS2ST1 physically interacts in the Golgi apparatus with glucuronyl c5-epimerase (5), which catalyzes the conversion of glucuronic acid to iduronic acid (6). As a consequence, 2-O sulfation predominantly occurs on iduronic acids naturally and overexpression of HS2ST1 alone causes an increase in 2-O sulfation on glucuronic acid (7). The enzyme activity of the recombinant human HS2ST1 was measured using a PAP-specific phosphatase-coupled sulfotransferase assay (8).

References

  1. Bernfield, M. et al. (1999) Annu. Rev. Biochem. 68:729.
  2. Esko, J.D. and Selleck, S.B. (2002) Annu. Rev. Biochem. 71:435.
  3. Kobayashi, M. et al. (1996) J. Biol. Chem. 271:7645.
  4. Bullock, S.L. et al. (1998) Genes & Development 12:1894.
  5. Li, J.P. et al. (2001) J. Biol. Chem. 276:20069.
  6. Pinhal, M.A.S et al. (2001) Proc. Natl. Acad. Sci. USA. 98:12984.
  7. Rong, J. et al. (2000) Biochem. J. 346:463.
  8. Prather, B. et al. (2012) Anal Biochem. 423:86.

Alternate Names

2OST

Entrez Gene IDs

9653 (Human)

Gene Symbol

HS2ST1

UniProt

Q7LGA3

Additional Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1 Products

Product Documents for Recombinant Human HS2ST1 Protein, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Human HS2ST1 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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