Prnp Antibody
产品详情
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产品名称:Rabbit anti-Rattus norvegicus (Rat) Prnp Polyclonal antibody
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Uniprot No.:P13852
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基因名:Prnp
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别名:Prnp antibody; Prn antibody; Prp antibody; Major prion protein antibody; PrP antibody; CD antigen CD230 antibody
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宿主:Rabbit
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反应种属:Rat
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免疫原:Recombinant Rat Major prion protein (29-231AA)
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免疫原种属:Rattus norvegicus (Rat)
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标记方式:Non-conjugated
本页面中的产品,Prnp Antibody (CSB-PA018739LA01RA),的标记方式是Non-conjugated。对于Prnp Antibody,我们还提供其他标记。见下表:
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克隆类型:Polyclonal
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抗体亚型:IgG
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纯化方式:>95%, Protein G purified
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浓度:It differs from different batches. Please contact us to confirm it.
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保存缓冲液:Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4 -
产品提供形式:Liquid
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应用范围:ELISA
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Protocols:
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储存条件:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
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货期:Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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靶点详情
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功能:Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.
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基因功能参考文献:
- the mechanism by which stressful stimuli induced by opiate withdrawal and the subsequent long-term homeostatic changes in hippocampal plasticity, modulate the expression and the dynamics of Prion protein. PMID: 28081197
- The results suggest a role of PrP(C) in proteostasis, dysfunctions of which may be involved in the pathogenesis of neurodegenerative diseases such as TSE and Alzheimer's Disease. PMID: 26946358
- this study implies that lithium, the commonly used mood stabilizer, may be a promising therapeutic agent in TSE, particularly in case of the disease forms associated with accumulation of cytoPrP. PMID: 26149502
- We provide the first report that mean PrPC concentration in primary blast exposed rats is significantly increased compared with controls PMID: 25058115
- data provide new insights into the cellular mechanism of prion conversion and suggest that GM1-prion protein interaction at the cell surface could play a significant role in the mechanism predisposing to pathology. PMID: 24859148
- The toxicity of PrP(111-126) to cultured astrocytes was reduced following the addition of Cu(2+) ions, owing to binding affinity of copper towards histidine moiety present in the peptide. PMID: 24386462
- Down regulation of brain cellular prion protein in an animal model of insulin resistance. PMID: 24780399
- PrP(106-126) cytotoxic amyloid oligomers disruption of membranes is dependent on bilayer composition PMID: 24554723
- Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1 PMID: 23386614
- The study suggests a pivotal role for PrP(C) in the cell adaptation to copper limitation through a direct activity of ion uptake. PMID: 22362149
- The prion protein and mrna was regulaion in vitamin B(12)rats. PMID: 22116041
- The nerves of the PrP(C)-treated rats show typical cobalamin-deficient lesions, significantly decreased abnormal maximum nerve conduction velocity values, and significantly increased tumor necrosis factor-alpha levels. PMID: 22102467
- mutant or cytosolic PrP expression in transgenic mice and human or rat cells is not associated with endoplasmic reticulum stress or proteasome dysfunction PMID: 21559407
- Data demonstrate that PrP(C) is abundant in the nuclear lamina of endocrine and neuronal cells and interacts with histone H1(0), histone H3 and lamin B1. PMID: 21277044
- These new data indicate that PrPc gene regulation is highly dependent on disruption of chromatin fiber assembly, which allows some ubiquitous transcription factors accession to specific DNA elements PMID: 11739375
- In retinal explants from neonatal mice and rats, engagement of PrP(c) transduces neuroprotective signals through a cAMP/PKA-dependent pathway. PrP(c) may function as a trophic receptor, the activation of which leads to a neuroprotective state. PMID: 12093733
- Two heat-shock elements (HSEs) were located at the positions of -680 bp (HSE1; GGAACTATTCTTGACATTGCT), and -1653 bp (HSE2; TGAGAACTCAGGAAG) of the rat PrP (RaPrP) gene promoter. PMID: 12392052
- PrP is not subject to retrotranslocation from the ER into the cytoplasm prior to degradation by the proteasome PMID: 12663673
- Various prion glycoforms in B104 neuroblastoma cells were tightly regulated as a function of cell density and during neuronal differentiation. Potential role of cellular prion protein in cell-cell interactions and differentiation. PMID: 12911750
- the intrinsic properties of PrP-(82-146) are dependent upon the integrity of the C-terminal region and account for the massive deposition of PrP amyloid in GSS PMID: 12970341
- Glycosylphosphatidylinositol-anchored prion protein and Thy-1 were largely clustered in separate domains on the neuronal surface; the lipid content of these membrane domains differed markedly PMID: 14660659
- Prion proteins are membrane protein, isolated from neuronal cells, along with Marcks and fyn. PMID: 14741357
- PRNP shows no direct CAGA box correspondence with the APP superfamily members. PMID: 15208260
- early association of PrP(C) with cholesterol-enriched rafts facilitates its correct folding PMID: 15229281
- We propose that this unusual beta-turn-rich form of PrP may be a precursor of PrPSc and a candidate for the neurotoxic molecule in prion pathogenesis. PMID: 15670783
- Immunostained cells expressing PrP(c) appear scattered throughout the epithelium of fundic and pyloric glands as well as in intestinal villi and crypts. PMID: 15891070
- These results indicate that DRMs are essential for proper trafficking and distribution of PrP(C) at late stages of neuronal differentiation and that its function, at least in hippocampus, is restricted to the axonal domain. PMID: 16139509
- Prnp expression is upregulated by copper in neuronal cells by an MTF-1-independent mechanism, and suggest a metal-specific modulation of Prnp in neurons PMID: 16148034
- prion protein plasma membrane environment in differentiated neurons resulted to be a complex entity, whose integrity requires a network of lipid-mediated non-covalent interactions PMID: 16248888
- Our results indicated a novel PrP(C) interacting protein and suggested that this complex might be relevant in modulating a variety of electrophysiological-dependent cellular responses PMID: 16750514
- J protein family serves as a 'folding catalyst' for PrP(C) and implicates Rdj2 as a factor in the protection against prion diseases PMID: 16774738
- Pronounced cytosolic aggregation of cellular prion protein in pancreatic beta-cells in response to hyperglycemia. PMID: 17146448
- Our findings show that, through its interaction with LN, hippocampal PrPc plays a critical role in memory processing and suggest that this role is mediated by activation of both PKA and ERK1/2 signaling pathways. PMID: 17156386
- PrP(106-126) aggregates in vitro and this aggregation state is important for its neurotoxicity PMID: 17405933
- the plasma membrane localization of PrP(C) and/or of the converted scrapie form might be necessary for the development of a symptomatic disease PMID: 17556367
- PrP(C) is widely expressed in a subset of neurons that contain markers of inhibitory populations of cells throughout the rat brain PMID: 17854776
- Results demonstrate by immunohistochemical analysis the colocalization of neuroglobin and PrP(c) in the retinal ganglion cell layer. PMID: 19327369
- Our data support a significant role for PrP(c) as a response mediator in neuritogenesis and cell differentiation. PMID: 19457127
- The peculiar lipid composition and, in particular, the presence of proteins involved in synaptic plasticity, cell adhesion, cytoskeleton regulation and signaling suggest an important physiological role for the PrPC prion domain in neurons. PMID: 19493159
- Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells PMID: 19503793
- distinct N-terminal cleavage products of PrP(c) harbor different biological activities underlying the various phenotypes linking PrP(c) to cell survival. PMID: 19850936
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相关疾病:Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
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亚细胞定位:Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus.
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蛋白家族:Prion family
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数据库链接:
KEGG: rno:24686
STRING: 10116.ENSRNOP00000028881
UniGene: Rn.3936
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