Product DescriptiongoogleRabbit anti-Presenilin 2 loop region Polyclonal Antibody (Unconjugated), suitable for WB, ICC.
Alternative NamesAD3LP, AD5, E5-1, STM-2
Application(s)ICC, WB
Antibody HostRabbit
Antibody TypePolyclonal
SpecificityConfirmed by Western blot using mouse and human brain and knock down of presenilin 2 in vitro using siRNA see ref 6 below. Not reactive with presenilin 1.
Species ReactivityHuman, Mouse
Immunogen DescriptionA synthetic peptide (KLDPSSQGALQLPYDPEMEEDSYDSFGEP-C) corresponding to human PS1 [306-334] in the loop region conjugated via additional C-terminal Cys to Diphtheria toxoid.
Product DescriptionRabbit anti-Presenilin 2 loop region Polyclonal Antibody (Unconjugated), suitable for WB, ICC.
Application(s)ICC, WB
Application DetailsWB and IP. Suggested dilution of 1:1,000 is recommended for WB. Full length presenilin 2 (448 aa) has relative MW of about 45 kDa, with this antibody most commonly detected as cleaved CTF of 22 kDa with this antibody. Human or mouse brain samples commonly prepared with reducing agent (50mM DTT), urea (2.3 M), SDS (1.5%) in 62.5 mM Tris-HCL pH 6.8 sample buffer (without boiling) heating to 50 C for 15 min. The suggested dilution for IP is 1:100 . Biosensis recommends that the optimal working dilution should be determined by the end user.
TargetPresenilin 2 loop region
SpecificityConfirmed by Western blot using mouse and human brain and knock down of presenilin 2 in vitro using siRNA see ref 6 below. Not reactive with presenilin 1.
Target Host SpeciesHuman
Species ReactivityHuman, Mouse
Antibody HostRabbit
Antibody TypePolyclonal
Antibody IsotypeIgG
ConjugateUnconjugated
Immunogen DescriptionA synthetic peptide (KLDPSSQGALQLPYDPEMEEDSYDSFGEP-C) corresponding to human PS1 [306-334] in the loop region conjugated via additional C-terminal Cys to Diphtheria toxoid.
Purity DescriptionProtein G purified IgG
FormatLyophilized from PBS, pH 7.4. Contains no preservative.
Reconstitution InstructionsSpin vial briefly before opening. Reconstitute in 500 µL sterile-filtered 1X PBS, pH 7.2-7.6. Centrifuge to remove any insoluble material.
Storage InstructionsShort term storage at 2-8°C for one week. At -20°C as an undiluted liquid for up to 12 months.
Batch NumberPlease see item label.
Expiration Date12 months after date of receipt (unopened vial).
Scientific BackgroundAutosomal 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.
Western Immunoblotting of mouse and human Presenilin 2 protein in mouse cell line extracts, various mouse tissues and a human cell line. Membrane proteins were prepared and loaded as 20 µg protein per lane. Crude anti-PS2 loop antibody used at 1:1000.
General ReferencesCulvenor, J.G., Ilaya, N.T., Ryan, M.T., Canterford, L., Hoke, D., Williamson, N.A., McLean, C.A., Masters, C.L., and Evin, G. (2004) Characterization of Presenilin complex from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with Presenilin mutations. Eur. J. Biochem. 271, 375-385. Ilaya, N.T., Evin, G., Masters, C.L., and Culvenor, J.G. (2004) Nicastrin expression in mouse peripheral tissues is not co-ordinated with Presenilin and is high in muscle. J. Neurochem. 91, 230-237. Beher, D., Fricker, M., Nadin, A., Clarke, E.E., Wrigley, J.D.J., Li, Y.-M., CULVENOR, J.G., Masters, C.L., Harrison, T., and Shearman, M.S. (2003) In vitro Characterization of the Presenilin-dependent _-secretase complex using a novel affinity ligand. Biochem. 42, 8133-8142. Evin, G., Smith, M.J., Tziotis, A., McLean, C., Canterford, L., Sharples, R.A., Cappai, R., Weidemann, A., Beyreuther, K., Cotton, R.G.H., Masters, C.L., and Culvenor, J.G. (2002) Alternative transcripts of Presenilin-1 associated with Frontotemporal Dementia. NeuroReport 13, 917-921. Evin, G., Sharples, R.A., Weidemann, A., Reinhard, F.B.M., Carbone, V., Culvenor, J.G., Holsinger, R.M.D., Sernee, M.F., Beyreuther, K., and Masters, C.L. (2001) Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease. Biochem. 40, 8359-836Greenough, M.A., Volitakis, I, Li, Q.-X., Laughton, K., Evin, G., Ho, M., Dalziel, A.H., Camakaris, J, Bush, A.I. (2011) Presenilins promote the cellular uptake of copper and zinc and maintain copper chaperone of SOD1-dependent copper/zinc superoxide dismutase activity. J. Biol Chem. 286, 9776-8