Recombinant Rat Major Prion Protein (PRNP) Protein (His)

Name: Recombinant Rat Major Prion Protein (PRNP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03447P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Major Prion Protein (PRNP) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13852
Target Symbol	PRNP
Synonyms	Prnp; Prn; Prp; Major prion protein; PrP; CD antigen CD230
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GGWNTGGSRYPGQGSPGGNRYPPQSGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWSQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMLHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS
Expression Range	29-231aa
Protein Length	Full Length of Mature Protein
Mol. Weight	26.3kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus.
Protein Families	Prion family
Database References	KEGG: rno:24686 STRING: 10116.ENSRNOP00000028881 UniGene: Rn.3936
Associated Diseases	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.

Gene Functions References

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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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