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G4171

Sigma-Aldrich

Anti-Glucocerebrosidase (C-terminal) antibody produced in rabbit

enhanced validation

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-D-glucosyl-N-acylsphingosine glucohydrolase, Anti-GBA, Anti-GBA1, Anti-Glucosidase, beta (Gluc), Anti-Glucosylceramidase (GlcCerase), Anti-Lysosomal glucocerebrosidase

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~60 kDa

species reactivity

human, mouse, rat

packaging

antibody small pack of 25 μL

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1 mg/mL

technique(s)

western blot: 1-2 μg/mL using HEK293-T cells lysate expressing human glucocerebrosidase (GBA)

UniProt accession no.

P04062

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GBA(2629)
mouse ... Gba(14466)

Related Categories

General description

Glucocerebrosidase is an enzyme having glucosylceramidase activity. Defect in lysosomal hydrolase glucocerebrosidase results in Gaucher disease. Mutation in GBA will retard or block the transport of GBA to endoplasmic reticulum. Anti-glucocerebrosidase (C-terminal) antibody can be used to incubate the SDS-PAGE gel. Anti-Glucocerebrosidase antibody reacts specifically with human GBA.

Immunogen

synthetic peptide corresponding to amino acids 517-536 of human glucocerebrosidase (GBA), conjugated to KLH. This sequence is identical in rat GBA and highly conserved in mouse GBA (single amino acid substitution).

Application

Anti-Glucocerebrosidase (C-terminal) antibody produced in rabbit has been used in
  • immunohistochemistry
  • immunoblot analysis

Anti-glucocerebrosidase (C-terminal) antibody can be used in western blotting and immunoblotting.

Biochem/physiol Actions

Glucocerebrosidase (GBA) activity is reduced in human with mutations in GBA gene and causes accumulation of glucosylceramide (GlcCer). Fibroblasts from patients with defined GBA mutations show either retarded or blocked transport of GBA in the endoplasmic reticulum. Mutations in the human GBA gene may contribute to the development of common age-related dementia known as dementia with Lewy bodies. Several studies indicate that mutations in the human GBA gene are associated with early-onset Parkinson disease.
Glucocerebrosidase is an enzyme having glucosylceramidase activity. Defect in lysosomal hydrolase glucocerebrosidase results in Gaucher disease. Mutation in GBA will retard or block the transport of GBA to endoplasmic reticulum.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Reducing GBA2 activity ameliorates neuropathology in Niemann-Pick type C mice
Marques ARA, et al.
Testing, 10(8), e0135889-e0135889 (2015)
Gaucher disease paradigm: From ERAD to comorbidity.
Inna Bendikov-Bar, Mia Horowitz
Human Mutation, 33(10), doi: 10-doi: 10 (2012)
Joseph R Mazzulli et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 36(29), 7693-7706 (2016-07-23)
Parkinson's disease (PD) is characterized by the accumulation of α-synuclein (α-syn) within Lewy body inclusions in the nervous system. There are currently no disease-modifying therapies capable of reducing α-syn inclusions in PD. Recent data has indicated that loss-of-function mutations in
Nahid Tayebi et al.
Molecular genetics and metabolism, 122(4), 198-208 (2017-11-28)
Mutations in GBA1 encountered in Gaucher disease are a leading risk factor for Parkinson disease and associated Lewy body disorders. Many GBA1 mutation carriers, especially those with severe or null GBA1 alleles, have earlier and more progressive parkinsonism. To model
Inna Bendikov-Bar et al.
Orphanet journal of rare diseases, 9, 86-86 (2014-06-18)
Parkinson's disease (PD) is a movement neurodegenerative disorder characterized by death of dopaminergic neurons in the substantia nigra pars compacta of the brain that leads to movement impairments including bradykinesia, resting tremor, postural instability and rigidity. Mutations in several genes
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