Recombinant Mouse Prion-Like Protein Doppel (PRND) Protein (His&Myc)

Name: Recombinant Mouse Prion-Like Protein Doppel (PRND) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-08672P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Prion-Like Protein Doppel (PRND) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9QUG3
Target Symbol	PRND
Synonyms	Prnd; Prion-like protein doppel; Doppelganger; Dpl; PrPLP
Species	Mus musculus (Mouse)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	RGIKHRFKWNRKVLPSSGGQITEARVAENRPGAFIKQGRKLDIDFGAEGNRYYAANYWQFPDGIYYEGCSEANVTKEMLVTSCVNATQAANQAEFSREKQDSKLHQRVLWRLIKEICSAKHCDFWLERG
Expression Range	27-155aa
Protein Length	Full Length of Mature Protein
Mol. Weight	18.9 kDa
Research Area	Neuroscience
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	Required for normal acrosome reaction and for normal male fertility. Can bind Cu(2+).
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor.
Protein Families	Prion family
Database References	KEGG: mmu:26434 STRING: 10090.ENSMUSP00000105798 UniGene: PMID: 24339999 Data suggest that glycosylation status of the prion protein and yet-to-be-identified proteases modulate internal C1 and C2 endoproteolysis of Doppel (doppelganger prion) and Shadoo (shadow of prion protein) in mouse neurons. PMID: 24286250 Data on residue secondary structure propensities suggest that novel beta-sheets of doppel protein (Prnd) and prion protein (Prnp) are formed by amino acids belonging to helices that are the least stable in the respective native structures. PMID: 24143866 This finding identifies a protein domain that plays a role in mediating Dpl-related toxicity. PMID: 23345215 Findings raise the possibility that Bax and caspase-3 feature in Dpl-mediated apoptosis. PMID: 22561161 These results indicated that Dpl was glycosylated in a cell type- and tissue-specific manner regardless of PrP(C), while PrP(C) endoproteolysis was modulated by Dpl expression. PMID: 21144827 ectopic expression of PrP-like protein Doppel in central neurons induces significant Purkinje cell death resulting in late-onset ataxia PMID: 19055638 We suggest a mechanism for Doppel-mediated Purkinje cell degeneration linked to reduced gene expression of proteins related to neuronal activity. PMID: 20219645 interaction between Dpl and PrPC occurs in lipid rafts and is dependent on the integrity of these membrane microdomains PMID: 19888917 Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease PMID: 11842265 Ectopic PrPLP/Dpl in the absence of PRNP is actively involved in the glial-cell activation in the brain. PMID: 11844868 Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation PMID: 11866533 absence causes male sterility PMID: 12110578 tested whether Doppel and PrP(C) share the same cell location, thereby sharing the same neighboring cell components, probably required to share the same cell function PMID: 12387871 Prion and doppel proteins bind to granule cells of the cerebellum, suggesting a scenario in which granule cells express a protein that mediates Dpl-induced neurodegeneration. PMID: 12446843 Dpl protein binds copper, which may serve to modulate the activity, stability, or localization of the Dpl protein PMID: 12482851 Doppel expression is not modified in scrapie-infected cells. PMID: 12586339 findings provide evidence that the N-terminal residues 23-88 of prion protein containing the unique octapeptide-repeat region is crucial for preventing Purkinje cell death in PrP deficient mice expressing Doppel in the neuron PMID: 12759361 The mechanism of toxicity involved stimulation of nitric oxide production via activation of the nitric oxide synthases, nNOS and iNOS. PMID: 12799144 transgenic mice selectively expressing Dpl in Purkinje cells showed ataxia and Purkinje cell loss that depended on the level of Dpl expression PMID: 15007176 Dpl compensates for the loss of Prion protein function in mutant mouse lines, but it does have an important anti-oxidant function necessary for sperm integrity and male fertility. PMID: 15161660 Data show that Doppel protein expressed by Purkinje cells itself is toxic to the cells, and that the neurotoxicity is stoichiometrically antagonized by prion protein. PMID: 15194501 Doppel interacts with the full-length laminin receptor precursor protein PMID: 15246873 Cis-acting elements at the -182/-177 (E box) and -108/-104 (CCAAT box) positions were identified as the main activators of the Prnd expression in testis PMID: 15358521 genetic studies show that N-terminal modules in PrPC offset pro-apoptotic activity of the Doppel helix B/B' region in mice PMID: 15459186 Purkinje cell degeneration in protein-deficient mice is associated with cerebellar Prnd protein. PMID: 15862314 These results indicate that Dpl elicited dose-dependently toxic effects on PrP-deficient cells without affecting on PrP-expressing cells, suggesting that the PrP-Dpl interaction can regulate cell death in a cell-autonomous manner. PMID: 15950943 Loss of cellular prion protein renders hippocampal neurons susceptible to ischemic insult in male but not female mice. Ectopic expression of prion protein-like protein/Doppel aggravates ischemic neuronal death in female prion protein-null mice. PMID: 16198494 Involvement of upstream stimulatory factor in regulation of the mouse Prnd gene coding for Doppel protein PMID: 16297464 Doppel is expressed early during ontogenesis, and is found in both germ cells and Sertoli cells. Doppel may play a physiological role in acrosome biogenesis. PMID: 16421231 Abnormal expression of PrPLP/doppel in PrP-knockout mice is caused by functional dissociation between the pre-mRNA machineries, in particular those of cleavage/polyadenylation and splicing. PMID: 17034959 PrP(c) is involved with a response mediated by inflammation (paw edema) and by visceral conditioning stimuli. PMID: 17433806 ectopic expression of doppel induces both BAX-dependent and BAX-independent pathways of cell death PMID: 17443816 The finding that discrete lesions within the central nervous systems induced marked modulation of immune function probably indicates the existence of a delicately balanced neural-endocrine network by PrP(C) and PrPLP/Doppel. PMID: 17498663 Results suggest that non-Bax-dependent pathways mediate the toxic effects of Dpl in Purkinje cells, highlighting a possible role for nonapoptotic mechanisms in the death of these neurons. PMID: 17569776 Mitral cell loss and gliosis induced by ectopic Dpl expression were probably associated with the late-onset olfactory deficits in Rikn Prnp-/- mice. PMID: 17611634 a possible model for the antagonistic interaction between PrP and Dpl PMID: 19158506 Prion protein paralog doppel protein interacts with alpha-2-macroglobulin PMID: 19536284

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Mouse Prion-Like Protein Doppel (PRND) Protein (His&Myc)

Recombinant Mouse Prion-Like Protein Doppel (PRND) Protein (His&Myc)

Product Overview

Target Details

FAQs