CHST11 Protein, Human (sf9, His)

CHST11 Protein catalyzes sulfate transfer to position 4 of the GalNAc residue in chondroitin, the main proteoglycan in cartilage and cell surfaces. It can sulfate Gal residues in desulfated dermatan sulfate, with a preference for GlcA->GalNAc units over IdoA->GalNAc units, and does not form 4,6-di-O-sulfated GalNAc when chondroitin sulfate C is the acceptor. CHST11 Protein, Human (sf9, His) is the recombinant human-derived CHST11 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of CHST11 Protein, Human (sf9, His) is 312 a.a., with molecular weight of ~43 KDa.

CHST11 protein serves as a catalyst in the sulfate transfer to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin, a critical step in the biosynthesis of chondroitin sulfate. Chondroitin sulfate is a prominent proteoglycan found in cartilage and widely distributed on cell surfaces and extracellular matrices. Additionally, CHST11 exhibits the ability to sulfate Gal residues in desulfated dermatan sulfate. Notably, it displays a preference for sulfating in the GlcA->GalNAc unit over the IdoA->GalNAc unit and does not generate 4, 6-di-O-sulfated GalNAc when utilizing chondroitin sulfate C as an acceptor. This specific sulfation activity contributes to the intricate and precise modification of chondroitin sulfate, underscoring CHST11's role in the regulation of cartilage composition and other extracellular matrices.

Human

Sf9 insect cells

C-His

Q9NPF2-2 (M36-E347)

50515  [NCBI]

Approximately 43 kDa.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.