Anti-Prion Protein Antibody, clone POM1

Evaluated by Western Blotting in Brain homogenate from a Tga20 mouse overexpressing Prnp versus brain homogenate from a ZH3/ZH3 control mouse lacking Prnp.

Western Blotting Analysis: 0.5 µg/mL of this antibody this antibody detected PrP in Brain homogenate from a Tga20 mouse overexpressing Prnp versus brain homogenate from a ZH3/ZH3 control mouse lacking Prnp.

Anti-Prion Protein, clone POM1, Cat. No. MABN2285, is a highly specific mouse monoclonal antibody that targets PrP and has been tested in ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, and Western Blotting..

Research Category
Neuroscience

Western Blotting Analysis: A representative lot detected Prion Protein in Western Blotting applications (Kuffer, A., et. al. (2016). Nature. 536(7617):464-8; Polymenidou, M., et. al. (2008). PLoS One. 3(12):e3872).

Immunofluorescence Analysis: A representative lot detected Prion Protein in Immunofluorescence applications (Kuffer, A., et. al. (2016). Nature. 536(7617):464-8).

Immunohistochemistry Analysis: A representative lot detected Prion Protein in Immunohistochemistry applications (Polymenidou, M., et. al. (2008). PLoS One. 3(12):e3872).

Immunoprecipitation Analysis: A representative lot detected Prion Protein in Immunoprecipitation applications (Polymenidou, M., et. al. (2008). PLoS One. 3(12):e3872).

ELISA Analysis: A representative lot detected Prion Protein in ELISA applications (Polymenidou, M., et. al. (2008). PLoS One. 3(12):e3872).

Clone POM1 detects major prion protein in Tga20 mice brain. It targets an epitope within C-terminal globular domain.

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Major prion protein (UniProt: P04925; also known as PrP, PrP27-30, PrP33-35C, CD230) is encoded by the Prnp (also known as Prn-p, Prp) gene (Gene ID: 19122) in murine species. PrP is highly expressed in the brain, lung, kidney and heart and low levels of expression are reported in the liver and spleen. It is found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as Kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), and transmissible mink encephalopathy (TME). In normal brain it may play a role in neuronal development and synaptic plasticity and may be required for neuronal myelin sheath maintenance and myelin homeostasis through acting as an agonist for ADGRG6 receptor. PrP can exist in either PrPc (c = cellular) or PrPsc (sc = Scrapie) form. PrPc is a glycoprotein normally found inserted in the plasma membrane by a glycosyl phosphatidylinositol (GPI) anchor and can be easily digested by proteases. It is composed mainly of alpha-helices. The PrPsc has more of a beta-sheet type structure and is highly resistant to the action of proteases. The prion proteins possess two N-linked glycosylation sites and may contain over 50 different sugars. The large size of the N-linked sugars enables them to shield two orthogonal faces of the protein almost completely and protect large regions of the protein surface from proteases. The PrPsc is shown to contain the same set of glycans as PrPc, but has a higher proportion of tri- and tetra-antennary sugars. Multiplication of prion protein appears to be slower in vivo than in vitro. It is shown that following proteinase K treatment, PrPc is completely digested, whereas PrPsc is only shortened to a 27-30 kDa fragment. (Ref.: Meisl, G., et al. (2021). Nat. Struct. Mol. Biol. 28(4); 365-372).

~35 kDa observed; 27.98 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

GST-tagged recombinant fragment corresponding to 209 amino acids from the internal region of murine major prion protein.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.