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Merck
모든 사진(3)

주요 문서

G4171

Sigma-Aldrich

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

enhanced validation

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

동의어(들):

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 코드:
12352203
NACRES:
NA.41
결합:
unconjugated
application:
WB
클론:
polyclonal
종 반응성:
human, mouse, rat
citations:
62
기술:
western blot: 1-2 μg/mL using HEK293-T cells lysate expressing human glucocerebrosidase (GBA)

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

양식

buffered aqueous solution

분자량

antigen ~60 kDa

종 반응성

human, mouse, rat

포장

antibody small pack of 25 μL

향상된 검증

recombinant expression
Learn more about Antibody Enhanced Validation

농도

~1 mg/mL

기술

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

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

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

일반 설명

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.

면역원

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).

애플리케이션

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.

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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

개인 보호 장비

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Lot/Batch Number

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문서 라이브러리 방문

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
Lysosomal enzyme glucocerebrosidase protects against Abeta1-42 oligomer-induced neurotoxicity
Choi S, et al.
Testing, 10(12), e0143854-e0143854 (2015)
N370S-GBA1 mutation causes lysosomal cholesterol accumulation in Parkinson's disease
Garcia-Sanz P, et al.
Movement Disorders, 32(10), 1409-1422 (2017)
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
Gaucher disease paradigm: From ERAD to comorbidity.
Inna Bendikov-Bar, Mia Horowitz
Human Mutation, 33(10), doi: 10-doi: 10 (2012)

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