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关于此项目
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
3F4, monoclonal
Application:
ELISA
immunohistochemistry (formalin-fixed, paraffin-embedded sections)
immunoprecipitation (IP)
western blot
immunohistochemistry (formalin-fixed, paraffin-embedded sections)
immunoprecipitation (IP)
western blot
Species reactivity:
hamster, human
Citations:
37
Technique(s):
ELISA: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable
Uniprot accession no.:
产品名称
抗朊病毒蛋白抗体,a.a.109-112,克隆3F4, clone 3F4, Chemicon®, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
3F4, monoclonal
species reactivity
hamster, human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2a
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PRNP(5621)
相关类别
Analysis Note
免疫组化(石蜡):
正常大脑中的朊病毒蛋白(目录号MAB1562)染色模式/形态。用pH 6.0的柠檬酸盐预处理组织。使用带有HRP-DAB的IHC-Select Detection将这批抗体稀释至1:500。免疫反应性主要表现为神经元的细胞体染色。
使用柠檬酸盐缓冲液,pH值6.0进行最佳染色,表位修复:人大脑
正常大脑中的朊病毒蛋白(目录号MAB1562)染色模式/形态。用pH 6.0的柠檬酸盐预处理组织。使用带有HRP-DAB的IHC-Select Detection将这批抗体稀释至1:500。免疫反应性主要表现为神经元的细胞体染色。
使用柠檬酸盐缓冲液,pH值6.0进行最佳染色,表位修复:人大脑
Application
免疫组化(石蜡):
先前批次的代表性图像。 使用柠檬酸盐缓冲液,pH值6.0进行最佳染色,表位修复:人脑
免疫组化(Kitamoto et al.,1987):
1:100-1:1,000*参见下面的方案。
必须通过使用以下程序之一对组织进行预处理,将表位重新暴露在固定的组织中:
a. 甲酸在室温下10分钟(Kitamoto et al.,1987)
b. 水解高压灭菌(Kitamoto et al.,1991)
c. 微波(BioGenex,San Ramon,CA)
蛋白质印迹:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:10,000-1:100,000稀释液。
免疫沉淀:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:10-1:100稀释液。
ELISA:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:100,000稀释液。
最佳工作稀释度必须由最终用户确定。
先前批次的代表性图像。 使用柠檬酸盐缓冲液,pH值6.0进行最佳染色,表位修复:人脑
免疫组化(Kitamoto et al.,1987):
1:100-1:1,000*参见下面的方案。
必须通过使用以下程序之一对组织进行预处理,将表位重新暴露在固定的组织中:
a. 甲酸在室温下10分钟(Kitamoto et al.,1987)
b. 水解高压灭菌(Kitamoto et al.,1991)
c. 微波(BioGenex,San Ramon,CA)
蛋白质印迹:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:10,000-1:100,000稀释液。
免疫沉淀:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:10-1:100稀释液。
ELISA:(Kascsak,R.J.,1991;Kascsak,R.J.,1987):
使用先前批次的1:100,000稀释液。
最佳工作稀释度必须由最终用户确定。
该抗朊病毒蛋白抗体,a.a.109-112,克隆3F4经验证可用于ELISA、IH、IH(P)、IP、WB检测朊病毒蛋白。
Biochem/physiol Actions
朊病毒蛋白,人、仓鼠和猫的109-112位氨基酸残基。不与任何其他哺乳动物物种的PrP反应。MAB1562对天然和变性形式的PrP具有反应性。已固定的组织或细胞需要重新暴露的表位(见下文)。识别蛋白酶敏感和蛋白酶抗性形式的PrP。
General description
12.3kDa
人们认为朊病毒会在多种哺乳动物中引起多种疾病,包括牛的牛海绵状脑病(BSE,也称为“疯牛病”)和人类的克雅氏病(CJD)。迄今为止假设的全部朊病毒疾病会影响大脑或其他神经组织的结构,而全部目前尚无法治愈,并被认为是致命的。朊病毒被假设通过异常折叠形成一种结构来感染和传播,这种结构能够将正常的蛋白质分子转化为异常结构形式。全部已知的朊病毒诱导淀粉样蛋白折叠的形成,其中蛋白聚合成由紧密堆积的β片组成的聚集体。这种改变的结构极其稳定,并在感染的组织中积累,导致细胞死亡和组织损伤。这种稳定性意味着朊病毒对化学和物理试剂的变性具有抵抗力,从而使这些颗粒的处置和遏制变得困难。
Immunogen
表位:a.a.109-112
Physical form
在含有 PBS 且不含防腐剂的缓冲液中纯化的小鼠单克隆 IgG2a。
形式:纯化
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Jacob I Ayers et al.
PLoS pathogens, 7(3), e1001317-e1001317 (2011-03-26)
Prion strains are characterized by differences in the outcome of disease, most notably incubation period and neuropathological features. While it is established that the disease specific isoform of the prion protein, PrP(Sc), is an essential component of the infectious agent
Francesca Properzi et al.
The Journal of general virology, 96(Pt 7), 1969-1974 (2015-03-26)
In most forms of prion diseases, blood is infectious, but detection by immunochemistry techniques of the only available marker of infection (the misfolded prion protein, PrPTSE) in blood remains elusive. We developed a novel method for the detection of PrPTSE
Michele Christine Landemberger et al.
Journal of neurochemistry, 145(5), 409-416 (2018-01-18)
Cellular prion protein (PrPC ) is widely expressed and displays a variety of well-described functions in the central nervous system (CNS). Mutations of the PRNP gene are known to promote genetic human spongiform encephalopathies, but the components of gain- or
Zuzana Krejciova et al.
The Journal of experimental medicine, 214(12), 3481-3495 (2017-11-17)
Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt-Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades. In this paper, we show that astrocytes derived
Qi Shi et al.
International journal of molecular medicine, 41(4), 2413-2419 (2018-02-03)
Normal prion protein (PrP) contains two cysteines at amino acids 179 and 214, which may form intra‑ and interpeptide disulfide bonds. To determine the possible effects of this disulfide bridge on the biochemical features of PrP, prokaryotic recombinant human wild‑type PrP
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