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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

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)

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)
Eun-Jin Bae et al.
Nature communications, 5, 4755-4755 (2014-08-27)
Deposition of α-synuclein aggregates occurs widely in the central and peripheral nervous systems in Parkinson's disease (PD). Although recent evidence has suggested that cell-to-cell transmission of α-synuclein aggregates is associated with the progression of PD, the mechanism by which α-synuclein
Inna Bendikov-Bar et al.
Blood cells, molecules & diseases, 50(2), 141-145 (2012-11-20)
Gaucher disease (GD) is characterized by accumulation of glucosylceramide in lysosomes due to mutations in the GBA1 gene encoding the lysosomal hydrolase β-glucocerebrosidase (GCase). The disease has a broad spectrum of phenotypes, which were divided into three different Types; Type
N370S-GBA1 mutation causes lysosomal cholesterol accumulation in Parkinson's disease
Garcia-Sanz P, et al.
Movement Disorders, 32(10), 1409-1422 (2017)
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