Goat Anti-Prion Protein (143-153) Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | P04156 |
Other Accession | NP_898902, 5621, 19122 (mouse), 24686 (rat) |
Reactivity | Human |
Predicted | Pig |
Host | Goat |
Clonality | Polyclonal |
Concentration | 100ug/200ul |
Isotype | IgG |
Calculated MW | 27661 Da |
Gene ID | 5621 |
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Other Names | Major prion protein, PrP, ASCR, PrP27-30, PrP33-35C, CD230, PRNP, ALTPRP, PRIP, PRP |
Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Goat Anti-Prion Protein (143-153) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PRNP |
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Synonyms | ALTPRP, PRIP, PRP |
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) (By similarity). 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 (By similarity). |
Cellular Location | Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. |
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Background
The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. Alternative splicing results in multiple transcript variants encoding the same protein.
References
Lack of association between PRNP M129V polymorphism and multiple sclerosis, mild cognitive impairment, alcoholism and schizophrenia in a Korean population. Choi IG, et al. Dis Markers, 2010 Jan 1. PMID 20592456.
Polymorphisms of the prion protein gene (PRNP) in a Serbian population. Dimitrijevi? R, et al. Int J Neurosci, 2010 Jul. PMID 20583902.
Intermediate phenotypes identify divergent pathways to Alzheimer's disease. Shulman JM, et al. PLoS One, 2010 Jun 21. PMID 20574532.
Prion protein expression and the M129V polymorphism of the PRNP gene in patients with colorectal cancer. Antonacopoulou AG, et al. Mol Carcinog, 2010 Jul. PMID 20564346.
Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties. Bishop MT, et al. Proc Natl Acad Sci U S A, 2010 Jun 29. PMID 20547859.
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