|Tested species reactivity||Bovine, Deer, Human, Sheep|
|Published species reactivity||Hamster, Sheep, Human|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Synthetic peptide corresponding to residues S(146) R P L I H F G S D Y E D R(159) of bovine PrP.|
|Storage buffer||1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay dependent|
|Immunohistochemistry (Paraffin) (IHC (P))||3-5 µg/ml|
|Western Blot (WB)||3-5 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
MA1-750 detects prion protein (PrP) protein from a variety of species that have the conserved n-IHFG-c epitope, including agriculturally important animal species such as sheep, bovine, deer, and elk. MA1-750 has been successfully used in Western blot, immunohistochemistry and ELISA procedures. By Western blot, this antibody detects a 33-35 kDa protein from normal animals and a 27-30 kDa protein which represents PrP in brain protease treated tissue extracts from infected animals. Immunohistochemical staining of PrP(Sc) in infected sheep brain with MA1-750 results in intense staining of the spongiform lesions. In immunohistochemical procedures this antibody detects only the PrP(Sc) and not PrP(C). The MA1-750 immunogen is a synthetic peptide corresponding to residues S(146) R P L I H F G S D Y E D R(159) of bovine PrP. This peptide (Cat. # PEP-051) is available for use in neutralization and control experiments. MA1-750 is known to specifically recognize a conserved epitope of the PrP(Sc) protein comprising the amino acids n-IHFG-c.
Cellular prion protein (PrPC) is a highly conserved, 33-35 kDa protease-sensitive, sialoglycoprotein of unknown function which is endogenously expressed in brain. Studies have shown this protein to be anchored to the external surface of the cell membrane by glycosyl phosphatidylinositol. A post-translationally altered, protease-resistant PrPC isoform ( PrP-Scrapie or PrPSc) of 27-30 kDa is found in association with several fatal neurodegenerative disorders collectively termed transmissible spongiform encephalopathies (TSEs). Deposition of PrPSc in the central nervous system is a reliable indication of a TSE. Prion diseases include scrapie in sheep and goats, bovine spongiform encephalopathy or "Mad Cow disease", and chronic wasting disease (CWD) in deer and elk. PrP is responsible for Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker (GSS) disease, Fatal Familial Insomnia (FFI), and Kuru in humans.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Differentiating blood samples from scrapie infected and non-infected hamsters by detecting disease-associated prion proteins using Multimer Detection System.
MA1-750 was used in ELISA to investigate the efficacy of a novel method for prion detection
|An SS,Lim KT,Oh HJ,Lee BS,Zukic E,Ju YR,Yokoyama T,Kim SY,Welker E||Biochemical and biophysical research communications (392:505)||2010|
Preclinical diagnosis of scrapie by immunohistochemistry of third eyelid lymphoid tissue.
MA1-750 was used in immunohistochemistry to perform preclinical diagnosis of scrapie by means of immunohistochemistry assay of third eyelid lymphoid tissue
|O'Rourke KI,Baszler TV,Besser TE,Miller JM,Cutlip RC,Wells GA,Ryder SJ,Parish SM,Hamir AN,Cockett NE,Jenny A,Knowles DP||Journal of clinical microbiology (38:3254)||2000|
The pattern of prion-related protein expression in the gastrointestinal tract.
MA1-750 was used in immunohistochemistry to investigate the involvement of epithelial cells in prion entry and pathogenesis
|Pammer J,Cross HS,Frobert Y,Tschachler E,Oberhuber G||Virchows Archiv : an international journal of pathology (436:466)||2000|
Preclinical detection of PrPSc in nictitating membrane lymphoid tissue of sheep.
MA1-750 was used in immunohistochemistry to detect prion protein in lymphoid nodules isolated from sheep nictitating membrane
|O'Rourke KI,Baszler TV,Parish SM,Knowles DP||The Veterinary record (142:489)||1998|