The CHST8 Antibody (PACO05031) is a polyclonal antibody specifically designed for research involving CHST8, a key enzyme involved in the biosynthesis of chondroitin sulfate. This antibody, raised in rabbits, exhibits high reactivity with human samples and is validated for use in a variety of applications, including Western blot and immunohistochemistry.CHST8, also known as carbohydrate sulfotransferase 8, plays a crucial role in the modification of glycosaminoglycans, which are important components of the extracellular matrix. By targeting CHST8 with this antibody, researchers can effectively detect and analyze the expression of this enzyme in various tissues and cell types.
This makes the CHST8 Antibody ideal for studies in glycobiology, cartilage development, and cancer research.The CHST8 Antibody offers a valuable tool for investigating the function and regulation of CHST8 in normal physiological processes and disease states. Understanding the role of CHST8 in chondroitin sulfate biosynthesis can provide insights into potential therapeutic strategies for conditions such as osteoarthritis, cancer metastasis, and neurodevelopmental disorders. By using this antibody, researchers can further elucidate the complex mechanisms underlying glycosaminoglycan biosynthesis and its impact on human health.
Antibody Name:
CHST8 Antibody (PACO05031)
Antibody SKU:
PACO05031
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:40000, WB:1:500-1:2000
Species Reactivity:
Human, Mouse, Rat
Immunogen:
Synthesized peptide derived from the C-terminal region of human GalNAc4ST-1.
Form:
Liquid
Storage Buffer:
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
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]
