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PRND is found on chromosome 20, approximately 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally similar. Additionally we are shipping Prion Protein 2 (Dublet) Antibodies (22) and Prion Protein 2 (Dublet) Kits (5) and many more products for this protein.
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Human PRND Protein expressed in Escherichia coli (E. coli) - ABIN1098521
Peoch, Guérin, Brandel, Launay, Laplanche: First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases. in Neuroscience letters 2000
Show all 2 references for ABIN1098521
results demonstrate that blocking doppel can control VEGF signaling in TECs and selectively inhibit tumor angiogenesis.
The association between the APOE (show APOE Proteins), CYP46 (show CYP46A1 Proteins), PRNP (show PRNP Proteins) and PRND genes and the profile of neuropsychiatric symptoms in Polish subjects with Alzheimer's disease and mild cognitive impairment, was evaluated.
in astrocytomas, Dpl undergoes different molecular processes that might constitute additional helpful tools to characterize the glial tumor progression
Cytotoxicity induced by the expression of Dpl and truncated PrP (show C4BPA Proteins) in neural derived cells are closely related with the apoptosis process.
expression pattern and biochemical characteristics in human tissues and in Chinese hamster ovary cells transfected with wild-type or variant human Dpl gene constructs
Doppel expression is not modified in the brains of patients with Creutzfeldt-Jakob disease.
human Doppel fails to interact with itself; Dpl and PrP (show C4BPA Proteins) are not related or are only marginally related with respect to their ligand binding behaviour
results demonstrate that Doppel and PrPc (show PRNP Proteins) co-patch extensively at the plasma membrane
Doppel interacts with the full-length laminin receptor precursor protein
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.
Results showed that the region -323/+32 (+1 is the transcription start site) represents the promoter region and contains positive cis (show CISH Proteins)-acting elements
the genomic structure of three genes, PRNP (show PRNP Proteins), PRND, and RASSF2 (show RASSF2 Proteins), within the syntenic region of the bovine genome is highly conserved in order and orientation.
in GC-1 spg cells, phosphorylation of p21 and N-terminal truncated PrP may play roles in the control of Dpl-induced apoptosis, which may benefit the physiological function of Dpl in the male reproduction system.
Data suggest that glycosylation status of the prion protein (show PRNP Proteins) and yet-to-be-identified proteases modulate internal C1 and C2 endoproteolysis of Doppel (doppelganger prion (show PRNP Proteins)) and Shadoo (shadow of prion protein (show SPRN Proteins)) in mouse neurons.
Data on residue secondary structure propensities suggest that novel beta-sheets of doppel protein (Prnd) and prion protein (Prnp (show PRNP Proteins)) are formed by amino acids belonging to helices that are the least stable in the respective native structures.
This finding identifies a protein domain that plays a role in mediating Dpl-related toxicity.
Findings raise the possibility that Bax (show BAX Proteins) and caspase-3 (show CASP3 Proteins) feature in Dpl-mediated apoptosis.
These results indicated that Dpl was glycosylated in a cell type- and tissue-specific manner regardless of PrP(C (show PRNP Proteins)), while PrP(C (show PRNP Proteins)) endoproteolysis was modulated by Dpl expression.
ectopic expression of PrP-like protein Doppel in central neurons induces significant Purkinje cell death resulting in late-onset ataxia (show USP14 Proteins)
We suggest a mechanism for Doppel-mediated Purkinje cell degeneration (show AGTPBP1 Proteins) linked to reduced gene expression of proteins related to neuronal activity.
interaction between Dpl and PrPC (show PRNP Proteins) occurs in lipid rafts and is dependent on the integrity of these membrane microdomains
Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease
This gene is found on chromosome 20, approximately 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally similar. The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that is found predominantly in testis. Mutations in this gene may lead to neurological disorders.
prion protein 2 (dublet)
, prion-like protein doppel
, prion gene complex, downstream
, prion protein dublet
, prion protein-like protein
, prion protein-like protein, doppel