Skip to main content

Human Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1 Alexa Fluor™ Plus 488-conjugated Antibody

R&D Systems, part of Bio-Techne | Catalog # FAB6335AFP488

Catalog #
Availability
Size / Price
Qty
Loading...
FAB6335AFP488-100UG

Key Product Details

Species Reactivity

Human

Applications

Western Blot

Label

Alexa Fluor Plus 488 (Excitation = 493 nm, Emission = 518 nm)

Antibody Source

Monoclonal Mouse IgG1 Clone # 738306

Product Specifications

Immunogen

Chinese hamster ovary cell line CHO-derived recombinant human Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1

Specificity

Detects human Heparan Sulfate 2-O-Sulfotransferase 1/HS2ST1 in ELISAs and Western blots.

Clonality

Monoclonal

Host

Mouse

Isotype

IgG1

Applications

Application
Recommended Usage

Western Blot

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Formulation

Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

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).

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.

Alternate Names

2OST

Entrez Gene IDs

9653 (Human)

Gene Symbol

HS2ST1

UniProt

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

Product Documents

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices


This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

For research use only

Loading...
Loading...
Loading...
Loading...