Ms X PrP

Species Reactivity	Key Applications	Host	Format	Antibody Type
B, M, Sh, Elk, Md	ELISA, WB, IHC	M	Purified	Monoclonal Antibody

Species Reactivity

Key Applications

Host

Format

Antibody Type

B, M, Sh, Elk, Md

ELISA, WB, IHC

Purified

Monoclonal Antibody

Description
Catalogue Number	MAB5424
Brand Family	Chemicon®
Trade Name	Chemicon
Description	Anti-Prion Protein Antibody
Alternate Names	PrP CD230

Description

Catalogue Number

MAB5424

Brand Family

Chemicon®

Trade Name

Chemicon

Description

Anti-Prion Protein Antibody

Alternate Names

PrP
CD230

Product Information
Format	Purified
Presentation	Purified immunoglobulin. Liquid in PBS. Contains no preservative.

Product Information

Format

Purified

Presentation

Purified immunoglobulin. Liquid in PBS. Contains no preservative.

Applications
Application	Anti-Prion Protein Antibody is an antibody against Prion Protein for use in ELISA, WB, IH.
Key Applications	ELISA Western Blotting Immunohistochemistry
Application Notes	Western blot: 1:50,000-1:200,000 Immunohistochemistry: 1:100-1:500. Epitope must be re-exposed in fixed tissue by pretreatment of tissue using one of the following procedures: a. formic acid for 10 minutes at room temperature b. hydrolytic autoclaving c. heat induced epitope retrieval ELISA: 1:20,000-1:50,000 Optimal working dilutions must be determined by end user.

Applications

Application

Anti-Prion Protein Antibody is an antibody against Prion Protein for use in ELISA, WB, IH.

Key Applications

ELISA
Western Blotting
Immunohistochemistry

Application Notes

Western blot: 1:50,000-1:200,000

Immunohistochemistry: 1:100-1:500. Epitope must be re-exposed in fixed tissue by pretreatment of tissue using one of the following procedures:

a. formic acid for 10 minutes at room temperature

b. hydrolytic autoclaving

c. heat induced epitope retrieval

ELISA: 1:20,000-1:50,000

Optimal working dilutions must be determined by end user.

Biological Information
Immunogen	Recombinant PrP amino acids 23-237.
Concentration	Please refer to the Certificate of Analysis for the lot-specific concentration.
Host	Mouse
Specificity	Reacts with prion protein (PrP) from bovine, sheep, mule deer, elk and mouse. The monoclonal recognizes both protease sensitive and protease resistant forms of PrP (after denaturing).
Isotype	IgG1
Species Reactivity	Bovine Mouse Sheep Elk Mule Deer
Antibody Type	Monoclonal Antibody
Entrez Gene Number	NM_000311.3 NM_001080121.1 NM_001080122.1 NM_001080123.1 NM_183079.2
Entrez Gene Summary	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.
Gene Symbol	PRNP CD230 PrP33-35C PRP ASCR PrP27-30 GSS CJD PRIP PrP PrPc MGC26679
UniProt Number	P04156
UniProt Summary	FUNCTION: SwissProt: P04156 # The physiological function of PrP is not known. SIZE: 253 amino acids; 27661 Da SUBUNIT: PrP has a tendency to aggregate yielding polymers called rods. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. PTM: The glycosylation pattern (the amount of mono-, di- and non- glycosylated forms or glycoforms) seems to differ in normal and CJD prion. DISEASE: SwissProt: P04156 # 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 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) [MIM:123400]. 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) [MIM:600072]. 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) [MIM:137440]. 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 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. & Defects in PRNP are the cause of kuru [MIM:245300]. 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 prion disease with protracted course [MIM:606688]; 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.SIMILARITY:SwissProt: P04156 ## Belongs to the prion family.

Biological Information

Immunogen

Recombinant PrP amino acids 23-237.

Concentration

Please refer to the Certificate of Analysis for the lot-specific concentration.

Host

Mouse

Specificity

Reacts with prion protein (PrP) from bovine, sheep, mule deer, elk and mouse. The monoclonal recognizes both protease sensitive and protease resistant forms of PrP (after denaturing).

Isotype

IgG1

Species Reactivity

Bovine
Mouse
Sheep
Elk
Mule Deer

Antibody Type

Monoclonal Antibody

Entrez Gene Number

Entrez Gene Summary

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.

Gene Symbol

PRNP
CD230
PrP33-35C
PRP
ASCR
PrP27-30
GSS
CJD
PRIP
PrP
PrPc
MGC26679

UniProt Number

P04156

UniProt Summary

FUNCTION: SwissProt: P04156 # The physiological function of PrP is not known.
SIZE: 253 amino acids; 27661 Da
SUBUNIT: PrP has a tendency to aggregate yielding polymers called rods.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
PTM: The glycosylation pattern (the amount of mono-, di- and non- glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
DISEASE: SwissProt: P04156 # 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 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) [MIM:123400]. 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) [MIM:600072]. 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) [MIM:137440]. 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 1 (HDL1) [MIM:603218]. HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features. & Defects in PRNP are the cause of kuru [MIM:245300]. 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 prion disease with protracted course [MIM:606688]; 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.SIMILARITY:SwissProt: P04156 ## Belongs to the prion family.

Product Usage Statements
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Product Usage Statements

Usage Statement

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	Maintain at -20°C to -70°C in undiluted aliquots for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles.

Storage and Shipping Information

Storage Conditions

Maintain at -20°C to -70°C in undiluted aliquots for up to 6 months after date of receipt.

Avoid repeated freeze/thaw cycles.

Packaging Information
Material Size	100 µg

Packaging Information

Material Size

100 µg

实验耗材

分子生物学试剂

蛋白与免疫学

生化试剂

细胞及检测试剂

色谱及层析

仪器设备

实验服务

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