Human Carbohydrate Sulfotransferase 15/CHST15 Antibody
Human Carbohydrate Sulfotransferase 15/CHST15 Antibody Summary
Accession # Q7LFX5
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Carbohydrate Sulfotransferase 15/CHST15
N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST or CHST15) is a type II transmembrane protein composed of a short N‑terminal cytoplasmic domain and a long C-terminal luminal catalytic domain. CHST15 transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the 6-O of GalNAc-4S on chondroitin sulfate A (CS-A) as well as dermatan sulfate (1), generating the chondroitin sulfate E (CS-E) disaccharide unit GlcA beta 1-3GalNAc-4S,6S. CS-E binds with strong affinity to Midkine, a heparan sulfate-binding growth factor (2), playing an important regulatory role in differentiation and morphogenesis during embryonic development. In situ hybridization for the expression of CHST15 in the postnatal mouse brain showed a widespread expression of the transcript in the developing brain except at postnatal day 7 (3). For comparison, chondroitin sulfate 6-O sulfotransferase-1 (C6ST-1) encoded by the CHST3 gene, only recognizes and transfers sulfate to the 6-O of unsulfated GalNAc residues on chondroitin sulfate generating the chondroitin sulfate C (CS-C) disaccharide unit GlcA beta 1-3GalNAc-6S (4). The sequence of the human CHST15 was found to be the same as human B-cell RAG-associated protein (BRAG) (1).
- Ohtake, S. et al. (2001) J. Biol. Chem. 276:43894.
- Zou, P. et al. (2003) Glycobiology 13:35.
- Purushothaman, A. et al. (2007) J. Biol. Chem. 282:19442.
- Thiele, H. et al. (2004) Proc. Natl. Acad. Sci. USA 101:10155.
- Robbins, P.W. (1962) Methods in Enzymol. 5:964.
- MacRae, I.J. et al. (2000) Biochemistry 39:1613.
- Wu, Z.L. et al. (2002) FASEB J. 16:539.
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