CHST5 Human
Description
CHST5 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (27-395 a.a.) and having a molecular mass of 42.9kDa.
CHST5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Carbohydrate Sulfotransferase 5 (CHST5) is an enzyme primarily located in the Golgi apparatus of specific cell types, including B cells, T cells, and intestinal epithelium. It plays a crucial role in the sulfation of keratan sulfate, a glycosaminoglycan found in the cornea. CHST5 facilitates the transfer of a sulfate group from a molecule called 3'-phospho-5'-adenylyl sulfate (PAPS) to the 6th position of non-reducing N-acetylglucosamine residues within keratan sulfate chains. This enzyme exhibits activity towards both short and long carbohydrate chains that possess poly-N-acetyllactosamine structures, specifically targeting the non-reducing terminal GlcNAc.
This recombinant CHST5 protein, of human origin, is produced using Sf9 Baculovirus cells. It exists as a single polypeptide chain that has undergone glycosylation and comprises 380 amino acids (specifically, amino acids 27 to 395). This corresponds to a molecular weight of 42.9 kDa. For purification purposes, the protein is engineered with a 6-amino acid His tag at its C-terminus and subsequently purified through proprietary chromatographic techniques.
The product is a colorless solution that has been sterilized by filtration.
The CHST5 protein is supplied in a solution with a concentration of 0.25 mg/ml. The solution also contains 20% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.
For short-term storage (up to 2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA to a final concentration of 0.1%. It's important to avoid subjecting the product to repeated cycles of freezing and thawing.
The purity of this protein is determined to be greater than 90.0% based on SDS-PAGE analysis.
The specific activity of this enzyme is measured to be greater than 10,000 pmol/min/µg. Specific activity is defined as the enzyme's capacity to transfer sulfate from PAPS to N-acetyl-D-glucosamine per minute at a pH of 7.5 and a temperature of 37°C.
Carbohydrate sulfotransferase 5, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4, GST4, Intestinal N-acetylglucosamine-6-O-sulfotransferase, I-GlcNAc6ST, Intestinal GlcNAc-6-sulfotransferase, mIGn6ST, N-acetylglucosamine 6-O-sulfotransferase 3, GlcNAc6ST-3, Gn6st-3, Chst5, Gst4.
Sf9, Baculovirus cells.
ADPEFSRQVP SSPAGLGERV HVLVLSSWRS GSSFVGQLFS QHPDVFYLME PAWHVWDTLS QGSAPALHMA VRDLIRSVFL CDMDVFDAYL PWRRNISDLF QWAVSRALCS PPVCEAFARG NISSEEVCKP LCATRPFGLA QEACSSYSHV VLKEVRFFNL QVLYPLLSDP ALNLRIVHLV RDPRAVLRSR EQTAKALARD NGIVLGTNGT WVEADPRLRV VNEVCRSHVR IAEAALHKPP PFLQDRYRLV RYEDLARDPL TVIRELYAFT GLGLTPQLQT WIHNITHGSG PGARREAFKT TSRDALSVSQ AWRHTLPFAK IRRVQELCGG ALQLLGYRSV HSELEQRDLS LDLLLPRGMD SFKWASSTEK QPESHHHHHH
Product Science Overview
Carbohydrate Sulfotransferase 5 (CHST5) is a member of the carbohydrate sulfotransferase family, which plays a crucial role in the sulfation of carbohydrates. This process is essential for various biological functions, including cell signaling, molecular recognition, and the structural integrity of tissues. CHST5 is particularly significant due to its involvement in the sulfation of N-acetylglucosamine (GlcNAc) residues, which are components of glycoproteins, proteoglycans, and glycolipids .
The CHST5 gene is located on chromosome 16 in humans and encodes a protein that is predominantly expressed in the colon and small intestine . The protein belongs to the Gal/GalNAc/GlcNAc 6-O-sulfotransferase (GST) family, which catalyzes the transfer of sulfate to position 6 of galactose (Gal), N-acetylgalactosamine (GalNAc), or N-acetylglucosamine (GlcNAc) residues .
CHST5 utilizes 3’-phospho-5’-adenylyl sulfate (PAPS) as a sulfonate donor to catalyze the transfer of sulfate to the non-reducing terminal GlcNAc residues and O-linked sugars of mucin-type acceptors . This sulfation process is critical for creating specific epitopes that can be recognized by extracellular matrix proteins, cell surface receptors, and viruses . The enzyme has a marked preference for sulfating O-linked sugars of mucin-type acceptors and does not transfer sulfate to longer carbohydrate substrates with poly-N-acetyllactosamine structures .
Carbohydrate sulfation, facilitated by CHST5, plays a vital role in various biological processes, including:
- Cell Signaling: Sulfated carbohydrates are involved in cell-cell communication and signaling pathways.
- Molecular Recognition: Sulfated epitopes are recognized by specific receptors, aiding in molecular recognition processes.
- Structural Integrity: Sulfation contributes to the structural integrity of tissues by modifying glycoproteins and proteoglycans .
Recombinant CHST5 proteins are used in research to study the enzyme’s function and its role in various biological processes. These recombinant proteins are typically produced in a carrier-free form to avoid interference from other proteins, such as Bovine Serum Albumin (BSA) . The recombinant form allows for detailed biochemical studies and the development of potential therapeutic applications.
