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FITC标记的朊病毒蛋白CD230抗体

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  • ¥2980
  • LMAI Bio
  • LM-11788R-FITC
  • 中国/美国/欧洲
  • 2026年05月29日
  • ICC=1:50-200 IF=1:50-200
  • Human, Mouse, Rat, Cow, Horse,
  • Human, Mouse, Rat, Cow, Horse,
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    • 详细信息
    • 询价记录
    • 文献和实验
    • 技术资料
    • 供应商

      上海联迈生物工程有限公司

    • 库存

      大量

    • 靶点

      详见说明书

    • 级别

      1

    • 目录编号

      LM-11788R-FITC

    • 克隆性

      多克隆

    • 抗原来源

      Rabbit

    • 保质期

      1年

    • 抗体英文名

      Anti-Prion protein PrP/CD230/FITC

    • 抗体名

      Anti-Prion protein PrP/CD230/FITC

    • 标记物

      FITC标记

    • 宿主

      Human, Mouse, Rat, Cow, Horse,

    • 适应物种

      Human, Mouse, Rat, Cow, Horse,

    • 免疫原

      详见说明书

    • 亚型

      IGg

    • 形态

      粉末、液体、冻干粉

    • 应用范围

      ICC=1:50-200 IF=1:50-200

    • 浓度

      1mg/ml

    • 保存条件

      -20 °C

    • 规格

      100ul

    FITC标记的朊病毒蛋白CD230抗体
    英文名称 Anti-Prion protein PrP/CD230/FITC
    中文名称 FITC标记的朊病毒蛋白CD230抗体
    别    名 AltPrP; ASCR; atal familial insomnia; CD230; CD230 antigen; CJD; Creutzfeld Jakob disease; Gerstmann-Strausler-Scheinker syndrome; GSS; KURU; Major prion protein; PRIO_HUMAN.  
    规格价格 100ul/2980元 购买        大包装/询价
    说 明 书 100ul  
    研究领域 细胞生物  神经生物学  干细胞  细菌及病毒  细胞表面分子  
    抗体来源 Rabbit
    克隆类型 Polyclonal
    交叉反应 Human, Mouse, Rat, Cow, Horse, 
    产品应用 ICC=1:50-200 IF=1:50-200  
    not yet tested in other applications.
    optimal dilutions/concentrations should be determined by the end user.
    分 子 量 25kDa
    细胞定位 细胞膜 
    性    状 Lyophilized or Liquid
    浓    度 1mg/ml
    免 疫 原 KLH conjugated synthetic peptide derived from human Prion protein PrP/CD230
    亚    型 IgG
    纯化方法 affinity purified by Protein A
    储 存 液 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
    保存条件 Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
    产品介绍 background:
    The function of PrP is still under debate. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro).

    Function:
    The function of PrP is still under debate. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G0/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro).

    Subunit:
    Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1. Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement (By similarity). Interacts with KIAA1191.

    Subcellular Location:
    Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus.

    Post-translational modifications:
    The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
    Isoform 2 is sumoylated by SUMO1.

    DISEASE:
    Note=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.
    Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD) [MIM:123400]. CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.
    Defects in PRNP are the cause of fatal familial insomnia (FFI) [MIM:600072]. FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.
    Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD) [MIM:137440]. GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.
    Defects in PRNP are the cause of kuru (KURU) [MIM:245300]. Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.
    Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF) [MIM:606688]; an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms.
    Prion diseases, or transmissible spongiform encephalopathies (TSEs), are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Characteristic of prion diseases, cellular PrP (PrPc) is converted to the disease form, PrPSc, through alterations in the protein folding conformations. PrPc is constitutively expressed in normal adult brain and is sensitive to proteinase K digestion, while the altered PrPSc conformation is resistant to proteases, resulting in a distinct molecular mass after PK treatment. Consistent with the transient infection process of prion diseases, incubation of PrPc with PrPSc both in vitro and in vivo produces PrPc that is resistant to protease degradation. Infectious PrPSc is found at high levels in the brains of animals affected by TSEs, including scrapie in sheep, BSE in cattle and Cruetzfeldt-Jakob disease in humans.

    Similarity:
    Belongs to the prion family.

    Database links:

    Entrez Gene: 281427 Cow

    Entrez Gene: 5621 Human

    Entrez Gene: 19122 Mouse

    Entrez Gene: 24686 Rat

    Entrez Gene: 493887 Sheep

    Omim: 176640 Human

    SwissProt: P10279 Cow

    SwissProt: P04156 Human

    SwissProt: P04925 Mouse

    SwissProt: P13852 Rat

    SwissProt: P23907 Sheep

    Unigene: 472010 Human

    Unigene: 610285 Human

    Unigene: 727471 Human

    Unigene: 648 Mouse

    Unigene: 3936 Rat



    Important Note:
    This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

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