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Merck
모든 사진(1)

주요 문서

P5999

Sigma-Aldrich

Monoclonal Anti-Prion Protein antibody produced in mouse

1 mg/mL, clone IPC1, purified immunoglobulin, buffered aqueous solution

동의어(들):

Anti-AA960666, Anti-CD230, Anti-PRIP, Anti-PrP, Anti-PrP<C>, Anti-PrPSc, Anti-Prn-i, Anti-RP23-401J24.1, Anti-Sinc

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

mouse

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

IPC1, monoclonal

양식

buffered aqueous solution

분자량

antigen 25-35 kDa

종 반응성

hamster, mouse, rat

농도

1 mg/mL

기술

microarray: suitable
western blot: 0.05-0.1 μg/mL using mouse brain extract

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

mouse ... Prnp(19122)
rat ... Prnp(24686)

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일반 설명

Monoclonal Anti-Prion Protein (mouse IgG1 isotype) is derived from the hybridoma IPC1 produced by the fusion of mouse myeloma cells (NSO cells) and splenocytes from PrP knock-out mice immunized with recombinant mouse PrPc.
Prion is a cell surface glycoprotein present in two isoform- PrPC (a cellular isoform) and PrPSc (a disease associated isoform). Prion Protein encodes a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. PrPC is found in the neurons of the brain and spinal cord. The prion protein is associated with several diseases like bovine spongiform encephalopathy, Creutzfeldt-Jakob disease and fatal familial insomnia.

면역원

recombinant mouse PrPC.

애플리케이션

Monoclonal Anti-Prion Protein antibody produced in mouse is useful in enzyme linked immunosorbent assay (ELISA), immunoblotting and immunoprecipitation.

생화학적/생리학적 작용

Prion protein (PrP) is a natural protein synthesized within the secretory pathway and transported to the surface of the cell where it is tethered to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. The activity of PrP is not well understood; it may be involved in copper utilization, serving to buffer copper at the synaptic cleft or to mediate re-uptake of copper into the presynapse. Alternatively, bound copper may influence PrP binding characteristics; the PrP-copper complex may be crucial for synaptic homeostasis as a result of its anti-oxidant activity. Prion plaques are of three types: unicentric (single, compact core), multicentric (two or more cores and definite border), and diffuse plaques without a definite central core.

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

10 - Combustible liquids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

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


가장 최신 버전 중 하나를 선택하세요:

시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Transplanted neural precursors enhance host brain-derived myelin regeneration.
Einstein O, et al.
The Journal of Neuroscience, 29(50), 15694-15702 (2009)
Prion and prejudice: normal protein and the synapse.
Brown DR.
Trends in Neurosciences, 24(2), 85-90 (2001)
Yaron Haviv et al.
Archives of neurology, 65(6), 762-775 (2008-06-11)
The misfolding and aggregation of specific proteins has emerged as a key feature of several neurodegenerative diseases. In prion diseases, progressive disease and neuronal loss are associated with the accumulation of PrP(Sc), the misfolded isoform of PrP(C). Previous in vitro
Microglia and the pathogenesis of spongiform encephalopathies.
Rezaie P and Lantos PL
Brain Research Reviews, 35(1), 55-72 (2001)
The cellular prion protein (PrP(C)): its physiological function and role in disease.
Westergard L
Biochimica et Biophysica Acta, 1772(6), 629-644 (2007)

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