Your Good Partner in Biology Research

  1. 首页
  2. 蛋白
  3. 重组蛋白
  4. Recombinant Rat Major prion protein (Prnp)

Recombinant Rat Major prion protein (Prnp)

In Stock Promotion
  • 中文名称：
    大鼠Prnp重组蛋白
  • 货号：
    CSB-EP018739RA
  • 规格：
    ￥1836
  • 促销：
    促销单品低至599元起
  • 图片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

产品详情

  • 纯度：
    Greater than 90% as determined by SDS-PAGE.
  • 基因名：
    Prnp
  • Uniprot No.：
  • 别名：
    Prnp; Prn; Prp; Major prion protein; PrP; CD antigen CD230
  • 种属：
    Rattus norvegicus (Rat)
  • 蛋白长度：
    Full Length of Mature Protein
  • 来源：
    E.coli
  • 分子量：
    26.3kDa
  • 表达区域：
    29-231aa
  • 氨基酸序列
    GGWNTGGSRYPGQGSPGGNRYPPQSGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWSQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMLHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白标签：
    N-terminal 6xHis-tagged
  • 产品提供形式：
    Liquid or Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 缓冲液：
    Tris-based buffer,50% glycerol
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    3-7 business days
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA：
    Please contact us to get it.

产品评价

靶点详情

  • 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.
  • 基因功能参考文献：
    1. 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
    2. 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
    3. 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
    4. We provide the first report that mean PrPC concentration in primary blast exposed rats is significantly increased compared with controls PMID: 25058115
    5. 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
    6. 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
    7. Down regulation of brain cellular prion protein in an animal model of insulin resistance. PMID: 24780399
    8. PrP(106-126) cytotoxic amyloid oligomers disruption of membranes is dependent on bilayer composition PMID: 24554723
    9. Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1 PMID: 23386614
    10. 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
    11. The prion protein and mrna was regulaion in vitamin B(12)rats. PMID: 22116041
    12. 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
    13. 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
    14. 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
    15. 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
    16. 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
    17. 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
    18. PrP is not subject to retrotranslocation from the ER into the cytoplasm prior to degradation by the proteasome PMID: 12663673
    19. 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
    20. 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
    21. 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
    22. Prion proteins are membrane protein, isolated from neuronal cells, along with Marcks and fyn. PMID: 14741357
    23. PRNP shows no direct CAGA box correspondence with the APP superfamily members. PMID: 15208260
    24. early association of PrP(C) with cholesterol-enriched rafts facilitates its correct folding PMID: 15229281
    25. 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
    26. 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
    27. 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
    28. 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
    29. 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
    30. 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
    31. 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
    32. Pronounced cytosolic aggregation of cellular prion protein in pancreatic beta-cells in response to hyperglycemia. PMID: 17146448
    33. 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
    34. PrP(106-126) aggregates in vitro and this aggregation state is important for its neurotoxicity PMID: 17405933
    35. 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
    36. PrP(C) is widely expressed in a subset of neurons that contain markers of inhibitory populations of cells throughout the rat brain PMID: 17854776
    37. Results demonstrate by immunohistochemical analysis the colocalization of neuroglobin and PrP(c) in the retinal ganglion cell layer. PMID: 19327369
    38. Our data support a significant role for PrP(c) as a response mediator in neuritogenesis and cell differentiation. PMID: 19457127
    39. 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
    40. Lipid rafts and clathrin cooperate in the internalization of PrP in epithelial FRT cells PMID: 19503793
    41. distinct N-terminal cleavage products of PrP(c) harbor different biological activities underlying the various phenotypes linking PrP(c) to cell survival. PMID: 19850936

    显示更多

    收起更多

  • 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.
  • 亚细胞定位：
    Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus.
  • 蛋白家族：
    Prion family
  • 数据库链接：

    KEGG: rno:24686

    STRING: 10116.ENSRNOP00000028881

    UniGene: Rn.3936