Overview

Description

  • NatureRecombinant
  • SourceWheat germ
  • Amino Acid Sequence
    • AccessionP04062
    • SpeciesHuman
    • SequenceSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKL KIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGS
    • Molecular weight36 kDa including tags
    • Amino acids146 to 235

Specifications

Our Abpromise guarantee covers the use of ab112290 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activityuseful for Antibody Production and Protein Array
  • Applications

    ELISA

    SDS-PAGE

    Western blot

  • FormLiquid
  • Additional Notesuseful for Antibody Production and Protein Array
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.79% Tris HCl, 0.31% Glutathione
    Note: Glutathione is reduced.

General info

  • Alternative names
    • Acid beta glucosidase
    • Acid beta-glucosidase
    • Alglucerase
    • Beta glucocerebrosidase
    • BETA GLUCOSIDASE, ACID
    • Beta-glucocerebrosidase
    • betaGC
    • D glucosyl N acylsphingosine glucohydrolase
    • D-glucosyl-N-acylsphingosine glucohydrolase
    • EC 3.2.1.45
    • GBA
    • Gba protein
    • GBA1
    • GC
    • GCase
    • GCB
    • GLCM_HUMAN
    • GLUC
    • Glucocerebrosidase
    • Glucocerebrosidase (alt.)
    • GLUCOCEREBROSIDASE PSEUDOGENE
    • Glucosidase beta
    • Glucosidase, beta, acid
    • Glucosidase, beta; acid (includes glucosylceramidase)
    • Glucosylceramidase
    • Imiglucerase
    • Lysosomal glucocerebrosidase
    • OTTHUMP00000033992
    • OTTHUMP00000033993
    see all
  • 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.
  • Target information above from: UniProt accession P04062 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Human GBA protein fragment images

  • ab112290 analysed on a 12.5% SDS-PAGE stained with Coomassie Blue.

References for Human GBA protein fragment (ab112290)

ab112290 has not yet been referenced specifically in any publications.

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