Monday, September 14, 2015

Biosensis’s Key Antibodies for Neurological Disease Research: Presenilins & Nicastrin

Biosensis has a number of highly published antibodies for your research into neurological diseases. Below we highlight four of our most popular Presenilin and Nicastrin antibodies

PRESENILIN


Rabbit polyclonal antibody to Presenilin 1 (1-20)
Presenilin-1 (PSEN1) is a multi-pass membrane protein and component of the gamma-secretase complex. PSEN1 is thought to play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. It may also play a role in hematopoiesis. Defects in PSEN1 are a cause of Alzheimer disease type 3 (AD3), a familial early-onset form of Alzheimer disease (Ref:SWISS-Prot).
Catalogue No.  R-1605-500 (Data SheetMSDS): A synthetic peptide corresponding to a region (1-20 aa) from the N-terminus of human Presenilin 1 conjugated to Diptheria toxoid.

Rabbit Polyclonal Presenilin 2 Loop Region
Autosomal dominant mutations in presenilin 2 are the second major cause of early-onset familial Alzheimer’s disease. Presenilin 2 is a multi-transmembrane protein which undergoes endoprotelysis to form an N-terminal fragment of about 29 kDa and C-terminal fragment of about 22 kDa. Presenilin 2 forms the catalytic core of the gamma-secretase complex which cleaves type 1 transmembrane proteins including the amyloid precursor protein to generate the C-terminus of the amyloid beta peptide.
Catalogue No.  R-1681-500 (Data SheetMSDS): A synthetic peptide (KLDPSSQGALQLPYDPEMEEDSYDSFGEP-C) corresponding to human PS1 [306-334] in the loop region conjugated via additional C-terminal Cys to Diphtheria toxoid.

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

Nicastrin, a type 1 membrane glycoprotein, is an essential component of the gamma secretase complex which is critical for the cleavage of the amyloid precursor protein and other membrane proteins. Nicastrin is widely expressed in different tissue types. This antibody reacts with immature forms of Nicastrin.

Rabbit polyclonal antibody to Nicastrin, central region
Detection of higher mol. wt. mature forms is likely to be blocked by glycosylation in this region of the protein.
Catalogue No.  R-1685-500 (Data SheetMSDS): A synthetic peptide (C-QGETFDYIGSSRMVYD) corresponding to human Nicastrin [331-346] in the central region conjugated via additional N-terminal Cys to Diphtheria toxoid.

Rabbit polyclonal antibody to Nicastrin, C-terminal domain
Catalogue No.  R-1684-500 (Data SheetMSDS): A synthetic peptide (C-NAKADVLFIAPREPGAVSY) corresponding to human Nicastrin [691-709] in the C-terminal region conjugated via additional N-terminal Cys to Diphtheria toxoid.


References
  1. 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.



Where can I find more information about Biosensis?

Visit the manufacturer page at www.stratech.co.uk/biosensis, email info@stratech.co.uk or call +44 (0) 1638 782600.

Stratech Scientific is a distributor of high quality, competitively priced, reliable products for research laboratories throughout the UK and Europe. Please contact us to find out which ranges we can supply in your country.
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