Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Suitable for: SDS-PAGE
Product nameRecombinant Mouse GBA protein (Tagged)
See all GBA proteins and peptides
Purity> 85 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceAQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRME LSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPT QKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLP EEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQ PGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLG FTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEA AKYVHGIAVHWYMDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQS VRLGSWDRGMQYSHSIITNLLYHVTGWTDWNLALNPEGGPNWVRNFVDSP IIVDIPKDAFYKQPMFYHLGHFSKFIPEGSQRVALVASESTDLETVALLR PDGSAVVVVLNRSSEDVPLTISDPDLGFLETVSPGYSIHTYLWRRQ
Predicted molecular weight72 kDa including tags
Amino acids20 to 515
Additional sequence informationFull length mature protein without the signal peptide (1-19aa). N-terminal 6xHis-SUMO-tagged.
Our Abpromise guarantee covers the use of ab235724 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
- Acid beta glucosidase
- Acid beta-glucosidase
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
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab235724 has not yet been referenced specifically in any publications.