Glucosylceramidase activbity assay
- Product name: Glucosylceramidase Activity Assay Kit (Fluorometric)
- Detection method: Fluorescent
- Example type: Cell lysate, tissue homogenate
- Test type: Enzyme activity (quantitative)
- Trial duration: Standard multi-step test
Product description
The Glucosylceramidase Activity Assay Kit (Fluorometric) (ab273339) provides a quick and easy way to monitor glucosylceramidase (GC) activity in a wide variety of biological samples. In this kit, glucosylceramidase cleaves a specific synthetic substrate and releases a fluorophore, which can be easily quantified (Ex / Em = 360/445 nm). The assay is specific, sensitive, and can detect as little as 0.2 µU of glucosylceramidase activity in a variety of samples.
Platform: Microplate
Properties
Storage instructions
Store at -20 ° C. See protocols.
Participation in the disease
GBA defects are the cause of Gaucher disease (GD) [MIM: 230800]; also known as glucocerebrosidase deficiency. GD is the most prevalent lysosomal storage disease, characterized by the accumulation of glucosylceramide in the reticuloendothelial system. Different clinical forms are recognized based on the presence (neuronopathic forms) or absence of central nervous system involvement, severity, and age of onset.
Defects in GBA are the cause of Gaucher disease type 1 (GD1) [MIM: 230800]; also known as adult non-neuronopathic Gaucher disease. GD1 is characterized by hepatosplenomegaly with consequent anemia and thrombopenia and bone involvement. The central nervous system is not involved.
Defects in GBA are the cause of Gaucher disease type 2 (GD2) [MIM: 230900]; also known as acute neuronopathic Gaucher disease. GD2 is the most severe form and is universally progressive and fatal. It manifests shortly after birth, and death usually occurs before patients reach two years of age.
Defects in GBA are the cause of Gaucher disease type 3 (GD3) [MIM: 231000]; also known as subacute neuronopathic Gaucher disease. GD3 has manifestations of the central nervous system. Defects in GBA are the cause of Gaucher disease type 3C (GD3C) [MIM: 231005]; also known as pseudo-Gaucher disease or Gaucher-like disease.
GBA defects are the cause of the perinatal lethality of Gaucher disease (GDPL) [MIM: 608013]. It is a distinct form of type 2 Gaucher disease, characterized by fetal onset. Hydrops details, fetal death in utero, and neonatal distress are prominent features. When there is no dropsy, neurological involvement begins in the first week and leads to death in three months. Hepatosplenomegaly is an important sign and is associated with ichthyosis, arthrogryposis, and facial dysmorphia.
Note
Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, generalized edema of the fetus with the accumulation of fluid in the body cavities due to non-immune causes. Nonimmune hydrops fetalis is not a diagnosis in itself, but rather a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
Defects in GBA contribute to susceptibility to Parkinson’s disease (PARK) [MIM: 168600]. A complex neurodegenerative disorder characterized by bradykinesia, tremor at rest, muscle stiffness, and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson’s disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
The disease is progressive and usually manifests after age 50, although cases of early-onset (before age 50) are known. Most cases are sporadic, suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients have a positive family history of the disease. Familial forms of the disease usually begin at an earlier age and are associated with atypical clinical features.
Sequence similarities
It belongs to the glycosyl hydrolase 30 families.
Cell location
Lysosome membrane. Interaction with saposin-C promotes membrane association.
