antibody

Goat anti-Prion Protein (143-153) Antibody

MBS421336

0.1 mg

300 USD

polyclonal

goat

nonconjugated

human, cow

western blot, enzyme immunoassay

Antibody

Goat anti-Prion Protein (143-153) Antibody

Prion Protein

PRNP; prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia); ASCR; CD230; CJD; GSS; MGC26679; PRIP; PrP; PrP27-30; PrP33-35C; PrPc; CD230 antigen; major prion protein; prion protein; prion p; PRNP antibody; prion protein (p27-30) (Creutzfeldt-Jakob disease; Gerstmann-Strausler-Scheinker syndrome; fatal familial insomnia) antibody; ASCR antibody; CD230 antibody; CJD antibody; GSS antibody; MGC26679 antibody; PRIP antibody; PrP antibody; PrP27-30 antibody; PrP33-35C antibody; PrPc antibody; CD230 antigen antibody; major prion protein antibody; prion protein antibody; prion protein (p27-30) (Creutzfeld-Jakob disease Gerstmann-Strausler-Scheinker syndrome; fatal familial insomnia) antibody; prion protein PrP antibody; prion-related protein antibody; Prion Protein; Prion Protein (143-153)

major prion protein preproprotein; Major prion protein; alternative prion protein; major prion protein; prion protein; ASCR; PrP27-30; PrP33-35C; CD_antigen: CD230

PRNP

PRNP; PRNP; CJD; GSS; PrP; ASCR; KURU; PRIP; PrPc; CD230; AltPrP; p27-30; PrP27-30; PrP33-35C; ALTPRP; PRIP; PRP; PrP

PRIO_HUMAN

Polyclonal

Goat

Tested: Human; Expected from sequence similarity: Human, Pig, Cow

253

SDYEDRYYREN

Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide

Supplied at 0.5 mg/ml in Tris saline, 0. 02% sodium azide, pH7.3 with 0.5% bovine serum albumin.

100ug specific antibody in 200ul

Aliquot and store at -20 degree C. Minimize freezing and thawing.

Peptide ELISA (EIA), Western Blot (WB)

Peptide ELISA: Antibody detection limit dilution 1: 64000. Western Blot: Approx 25kDa band observed in Human Brain lysates (calculated MW of 27.7kDa according to NP_000302.1 and NP_898902.1). Recommended concentration: 0.3-1ug/ml.

Immunogen: Peptide with sequence C-SDYEDRYYREN, from the internal region of the protein sequence according to NP_000302.1. Epitope: Internal region

Note: Reported variants represent identical protein (NP_000302.1; NP_898902.1; NP_001073590.1; NP_001073591.1; NP_001073592.1).

4506113

NP_000302.1

NM_000311.3

8,691 Da

Axon Guidance Pathway (1270303); Developmental Biology Pathway (1270302); Glypican 1 Network Pathway (138010); NCAM Signaling For Neurite Out-growth Pathway (1270312); NCAM1 Interactions Pathway (1270313); Prion Diseases Pathway (101144); Prion Diseases Pathway (100065)

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. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]

PRNP: May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. 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. PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD). CJD occurs primarily as a sporadic disorder (1 per million), while 10-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness. Defects in PRNP are the cause of fatal familial insomnia (FFI). FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia. Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD). GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 100 million live births. Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1). HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. Defects in PRNP are the cause of kuru (KURU). Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset. Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF); an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms. Belongs to the prion family. 2 isoforms of the human protein are produced by alternative initiation. Protein type: Membrane protein, GPI anchor; Microtubule-binding. Chromosomal Location of Human Ortholog: 20p13. Cellular Component: cell surface; cytoplasm; endoplasmic reticulum; extrinsic to membrane; Golgi apparatus; integral to membrane; lipid raft; mitochondrial outer membrane; nucleus; plasma membrane. Molecular Function: ATP-dependent protein binding; chaperone binding; copper ion binding; identical protein binding; lamin binding; microtubule binding; protein binding; tubulin binding. Biological Process: cell cycle arrest; cellular copper ion homeostasis; learning and/or memory; metabolic process; negative regulation of activated T cell proliferation; negative regulation of apoptosis; negative regulation of interferon-gamma production; negative regulation of interleukin-17 production; negative regulation of interleukin-2 production; negative regulation of protein amino acid phosphorylation; negative regulation of T cell receptor signaling pathway; negative regulation of transcription factor activity; protein homooligomerization; regulation of protein localization; response to cadmium ion; response to oxidative stress. Disease: Creutzfeldt-jakob Disease; Fatal Familial Insomnia; Gerstmann-straussler Disease; Huntington Disease-like 1; Kuru, Susceptibility To; Spongiform Encephalopathy With Neuropsychiatric Features

0.1 mg

300 USD