Product nameAnti-GBA antibody
See all GBA primary antibodies
DescriptionRabbit polyclonal to GBA
Tested applicationsSuitable for: Flow Cyt, IHC-P, WBmore details
Species reactivityReacts with: Mouse, Human
Predicted to work with: Cow, Pig
Synthetic peptide within Human GBA aa 337-365 (internal sequence) conjugated to Keyhole Limpet Haemocyanin (KLH). The exact sequence is proprietary.
Database link: P04062
- WB: Mouse lung tissue lysate. IHC-P: Human skin tissue. Flow Cyt: NCI-H460 cells.
Storage instructionsShipped at 4°C. Store at 4°C (up to 6 months). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.09% Sodium azide
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThis antibody is purified through a protein A column, followed by peptide affinity purification.
- Pathways and Processes
- Metabolic signaling pathways
- Lipid and lipoprotein metabolism
- Lipid metabolism
- Pathways and Processes
- Metabolic signaling pathways
- Energy transfer pathways
- Energy Metabolism
Our Abpromise guarantee covers the use of ab175869 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Flow Cyt||1/10 - 1/50.
ab171870 - Rabbit polyclonal IgG, is suitable for use as an isotype control with this antibody.
|IHC-P||1/50 - 1/100.|
Involvement in diseaseDefects in GBA are the cause of Gaucher disease (GD) [MIM:230800]; also known as glucocerebrosidase deficiency. GD is the most prevalent lysosomal storage disease, characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Different clinical forms are recognized depending 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 soon after birth, with death generally occurring 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 central nervous manifestations.
Defects in GBA are the cause of Gaucher disease type 3C (GD3C) [MIM:231005]; also known as pseudo-Gaucher disease or Gaucher-like disease.
Defects in GBA are the cause of Gaucher disease perinatal lethal (GDPL) [MIM:608013]. It is a distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism.
Note=Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but 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 disease (PARK) [MIM:168600]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson 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 the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.
Sequence similaritiesBelongs to the glycosyl hydrolase 30 family.
Cellular localizationLysosome membrane. Interaction with saposin-C promotes membrane association.
- Information by UniProt
- Acid beta glucosidase antibody
- Acid beta-glucosidase antibody
- Alglucerase antibody
Anti-GBA antibody (ab175869) + Mouse Lung Lysate at 35 µg
Developed using the ECL technique.
Observed band size: 56 kDa why is the actual band size different from the predicted?
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human skin labelling GBA with ab175869. A peroxisae-conjugated anti-rabbit IgG was used as the secondary antibody, followed by DAB staining.
Flow Cytometry analysis of NCI-H460 cells labelling GBA (green) with ab175869, compared to a negative control cell (blue). A FITC-conjugated goat-anti-rabbit IgG was used as the secondary antibody.
This product has been referenced in:
- Clarke E et al. Age-related neurochemical and behavioural changes in D409V/WT GBA1 mouse: Relevance to lewy body dementia. Neurochem Int 129:104502 (2019). Read more (PubMed: 31299418) »
- Atashrazm F et al. Reduced glucocerebrosidase activity in monocytes from patients with Parkinson's disease. Sci Rep 8:15446 (2018). Read more (PubMed: 30337601) »