The CHST8 Polyclonal Antibody (PACO22229) is a valuable tool for researchers studying CHST8, a key enzyme involved in the biosynthesis of glycosaminoglycans. This antibody, produced in rabbits, is highly specific for human samples and has been validated for use in Western blot applications. It binds to the CHST8 protein, allowing for accurate detection and analysis in a variety of cell types.CHST8 is essential for the proper functioning of glycosaminoglycans, which are critical components of the extracellular matrix and play a role in cell signaling, adhesion, and migration. Dysregulation of CHST8 has been implicated in various diseases, including cancer and developmental disorders.
By studying the expression and activity of CHST8, researchers can gain insights into the molecular mechanisms underlying these conditions and potentially identify new therapeutic targets.The CHST8 Polyclonal Antibody is a valuable tool for investigating the role of CHST8 in health and disease, making it a valuable asset for researchers in the fields of biochemistry, molecular biology, and biomedicine. Its high specificity and sensitivity make it an ideal choice for experiments aimed at elucidating the functions of CHST8 and its potential implications for human health.
Antibody Name:
CHST8 Antibody (PACO22229)
Antibody SKU:
PACO22229
Size:
100ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:3000
Species Reactivity:
Human
Immunogen:
Synthesized peptide derived from internal of human CHST8.
Form:
Liquid
Storage Buffer:
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extracts from K562 cells, using CHST8 antibody.
Background:
Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin.
CHST8: Catalyzes the transfer of sulfate to position 4 of non- reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin. CHST8 mutations may be a cause of generalized non- inflammatory peeling skin syndrome type A (PubMed:22289416). Peeling skin syndrome (PSS) is a genodermatosis characterized by continuous shedding of the outer layers of the epidermis. Two main PSS subtypes have been suggested. Patients with non-inflammatory PSS (type A) manifest white scaling, with painless and easy removal of the skin, irritation when in contact with water, dust and sand, and no history of erythema, pruritis or atopy. Inflammatory PSS (type B) is associated with generalized erythema, pruritus and atopy. It is an ichthyosiform erythroderma characterized by lifelong patchy peeling of the entire skin with onset at birth or shortly after. Several patients have been reported with high IgE levels. Belongs to the sulfotransferase 2 family.Protein type: Transferase; EC 2.8.2.-; Membrane protein, integralChromosomal Location of Human Ortholog: 19q13.1Cellular Component: Golgi membraneMolecular Function: N-acetylgalactosamine 4-O-sulfotransferase activityBiological Process: hormone biosynthetic process; proteoglycan biosynthetic process; sulfur metabolic processDisease: Peeling Skin Syndrome 3
UniProt Protein Details:
NCBI Summary:
The protein encoded by this gene belongs to the sulfotransferase 2 family. It is predominantly expressed in the pituitary gland, and is localized to the golgi membrane. This protein catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. It is responsible for sulfation of GalNAc on luteinizing hormone (LH), which is required for production of the sex hormones. Mice lacking this enzyme, exhibit increased levels of circulating LH, and precocious sexual maturation of both male and female mice. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Aug 2011]