Rabbit Prnp Polyclonal Antibody | anti-PRNP antibody

Prnp Antibody - middle region

Cat. Num. AAA3215911

• Reactivity: Cow, Dog, Goat, Human, Rat, Sheep
• Applications: Western Blot, Immunohistochemistry
• Purity: Affinity Purified
• Synonyms: Prnp; Polyclonal Antibody; Prnp Antibody - middle region; anti-PRNP antibody

• Host: Rabbit
• Reactivity: Cow, Dog, Goat, Human, Rat, Sheep
• Clonality: Polyclonal
• Purity/Purification: Affinity Purified
• Form/Format: Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
• Sequence: Synthetic peptide located within the following region: GGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHF
• Sequence Length: 254

• Applicable Applications for anti-PRNP antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Homology: Cow: 100%; Dog: 100%; Goat: 100%; Human: 100%; Rat: 100%; Sheep: 100%
• Immunogen: The immunogen is a synthetic peptide directed towards the middle region of Mouse Prnp
• Preparation and Storage: For short term use, store at 2-8 degree C up to 1 week. For long term storage, store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Immunohistochemistry (IHC)

(Rabbit Anti-PRNP AntibodyFormalin Fixed Paraffin Embedded Tissue: Human Testis TissueObserved Staining: Plasma membrane and cytoplasm in Leydig cellsPrimary Antibody Concentration: 1:100Other Working Concentrations: 1:600Secondary Antibody: Donkey anti-Rabbit-Cy3Secondary Antibody Concentration: 1:200Magnification: 20XExposure Time: 0.5 - 2.0 sec)

Western Blot (WB)

(Host: RabbitTarget Name: PrnpSample Type: Mouse Kidney lysatesAntibody Dilution: 1.0ug/ml)

Related Product Information for anti-PRNP antibody

This is a rabbit polyclonal antibody against Prnp. It was validated on Western Blot

Target Description: Prnp may play a role in neuronal development and synaptic plasticity, may be required for neuronal myelin sheath maintenance and may play a role in iron uptake and iron homeostasis. Prnp is a 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. It also provides Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.

Product Categories/Family for anti-PRNP antibody

Polyclonal; Developmental Biology; Apoptosis

NCBI and Uniprot Product Information

• NCBI GI #: 13173473
• NCBI GeneID: 19122
• NCBI Accession #: NP_035300
• NCBI GenBank Nucleotide #: NM_011170
• UniProt Accession #: P04925
• Molecular Weight: 28kDa
• NCBI Official Full Name: major prion protein
• UniProt Protein Name: Major prion protein
• Protein Family: Major prion protein
• UniProt Gene Name: Prnp
• UniProt Synonym Gene Names: Prn-p; Prp; PrP
• UniProt Entry Name: PRIO_MOUSE

Uniprot Description

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: Microtubule-binding; Membrane protein, GPI anchor

Cellular Component: Golgi apparatus; mitochondrial outer membrane; cell surface; membrane; cell; endoplasmic reticulum; cytoplasm; plasma membrane; lipid raft

Molecular Function: tubulin binding; ATP-dependent protein binding; identical protein binding; protein binding; copper ion binding; metal ion binding; chaperone binding; microtubule binding

Biological Process: cellular copper ion homeostasis; negative regulation of activated T cell proliferation; negative regulation of transcription factor activity; negative regulation of T cell receptor signaling pathway; negative regulation of interleukin-2 production; learning and/or memory; response to cadmium ion; regulation of protein localization; negative regulation of interleukin-17 production; response to copper ion; negative regulation of protein amino acid phosphorylation; negative regulation of interferon-gamma production; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; response to oxidative stress; protein homooligomerization; negative regulation of apoptosis