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Biosensis offers high-quality monoclonal and polyclonal antibodies for a variety of research applications.
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ANTIBODIES FOR NEUROLOGICAL DISEASE RESEARCH:
PRESENILINS AND NICASTRIN
Use the antibodies that your colleagues are using:
Biosensis has a number of highly published antibodies for your research into neurological diseases. In this newsletter we are highlighting three of our most popular Presenilin and Nicastrin antibodies.
There are many more great products for the study of Alzheimer's and Parkinson's disease. Check them out here.
Rabbit Polyclonal Presenilin 1 Antibody Rabbit Polyclonal Presenilin 2 Loop Region
Figure 1. Immunofluorescence analysis of Presenilin 1 with IgG-purified rabbit antibody raised against the N-terminal region (1-20) of PS1 protein (Cat# R-1605-500). PS1-positive and knock-out neurosphere-derived cells after differentiation were fixed with paraformaldehyde (15 min) and stained with R-1605-500 (20μg/ml). An antibody against the loop region of Presenilin 1 (Cat# R-1680-500) is also available.
Figure 2.
Western immunoblotting of mouse and human Presenilin 2 protein in mouse cell line extracts, various mouse tissues and a human cell line with rabbit anti-Presenilin 2 antibody (Cat# R-1681-500). Membrane proteins were prepared and loaded as 20 µg protein per lane. Whole serum anti-PS2 loop antibody was used at 1:1000 dilution. CTF: C-terminal fragment.
References:
1. M.X. Silveyra et al (2008) Presenilin-1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation. Mol. Cell Biol. 210, 788-792.
2. J.G. Culvenor et al (2004) Characterization of Presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations. Eur. J. Biochem. 271, 375-385.
3. N.T. Ilaya et al (2004) Nicastrin expression in mouse peripheral tissues is not co-ordinated with Presenilin and is high in muscle. J. Neurochem. 91, 230-237.
4. D. Beher et al (2003) In vitro Characterization of the Presenilin-dependent gamma-secretase complex using a novel affinity ligand. Biochem. 42, 8133-8142.
5. G. Evin et al (2002) Alternative transcripts of Presenilin-1 associated with Frontotemporal Dementia. NeuroReport 13, 917-921.
6. G. Evin et at (2001) Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease. Biochem. 40, 8359-8368.
NICASTRIN:
Rabbit Polyclonal Nicastrin C-Terminal (691-709) and Central Region (334-346) Antibodies
Figure: Western immunoblotting analysis of mouse Nicastrin protein in PS1-deficient cell line and adult mouse brain with Nicastrin central region antibody (Cat# R-1685-500, right panel) and C-terminal Nicastrin antibody (Cat# R-1684-500, left panel). Membrane proteins were prepared and loaded as 20 µg protein per lane.
References:
1. J.G. Culvenor et al (2004) Characterization of Presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic Presenilin mutations. Eur. J. Biochem. 271, 375-385.
2. N.T. Ilaya et al (2004) Nicastrin expression in mouse peripheral tissues is not co-ordinated with Presenilin and is high in muscle. J. Neurochem. 91, 230-237.3. D. Beher et al (2003) In vitro Characterization of the Presenilin-dependent gamma-secretase complex using a novel affinity ligand. Biochem. 42, 8133-8142.
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Biosensis delivers antibodies of the highest quality to the research community. Please visit our website for a full range of antibodies.
If you have a query on any of our products, one of our experienced researchers can help at biospeak@biosensis.com.
Until next time, good luck with your research.
Sincerely,
The Biosensis Team
Contact Information
Biosensis Pty Ltd
Address: 40-46 West Thebarton Road
Thebarton SA 5031 Australia
Email: info@biosensis.comPhone: +61 8 8352 7711 - In the United States, call us in California toll free on 1800 605-5127
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