Western blotting analysis of Creutzfeld-Jakob disease (CJD) negative (lane 1, 2) and CJD positive (lane 3, 4) human brain material using anti-PrP monoclonal antibody (MA1-10152). CJD positive patient has proteinase K resistent prion protein. Lane 1, 4: Samples with proteinase K treatment Lane 2, 3: Samples without proteinase K treatment
|Tested species reactivity||Human|
|Host / Isotype||Mouse / IgG2a|
|Immunogen||Recombinant human prion protein|
|Storage buffer||PBS, pH 7.4|
|Contains||15mM sodium azide|
|Storage Conditions||4° C, do not freeze|
|Tested Applications||Dilution *|
|Western Blot (WB)||0.5 ug/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.
This antibody recognizes human prion protein (PrP). The diglycosylated form of PrP has a MW of ~40 kDa, monoglycosylated form ~30 kDa, and nonglycosylated form ~19-21 kDa. This antibody is suitable for discrimination between normal cellular prion protein (PrPc) and its conformationally changed form (PrPSc) prion protein.
CD230 / Human prion protein (PrP), also known as PRNP, is a ubiquitously expressed GPI-anchored cell surface glycoprotein associating with lipid raft components and functioning as a signaling molecule. CD230 / PrP plays a role in apoptosis in a cell context-dependent manner, is involved in proliferation of epithelial cells and in distribution of junction-associated proteins in human enterocytes. Conversion of this normal cellular prion protein (PrPc) into an abnormal conformer (PrPSc) is the crucial step associated with triggering the pathogenesis of the prion neurodegenerative disorders, such as the Creutzfeld-Jakob disease (CJD). Whereas PrPc is rich in alpha-helices, the PrPSc form has higher content of beta-sheets and is resistant to proteinase K.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.