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Biosensis/Rabbit polyclonal antibody to Presenilin 2 loop region: IgG/R-1681-500/500 ug
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Description 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. Batch No. See product label Unit size 500 ug Antigen A synthetic peptide (KLDPSSQGALQLPYDPEMEEDSYDSFGEP-C) corresponding to human PS1 [306-334] in the loop region conjugated via additional C-terminal Cys to Diphtheria toxoid. Antibody Type Polyclonal Other Names AD3LP, AD5, E5-1, STM-2 Produced in Rabbit Applications WB 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. Specificity Confirmed 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 Against Human; mouse; rat; guinea pig. Presenilin proteins are highly conserved, so cross-reactivity with other species is expected. Form Lyophilized from PBS, pH 7.4. Contains no preservative. Reconstitution Reconstitute in 500 µL of sterile water. Centrifuge to remove any insoluble material. Storage Short term storage at 2-8°C for one week. At -20°C as an undiluted liquid for up to 12 months. Expiry Date 12 months after purchase References Culvenor, J.G., Ilaya, N.T., Ryan, M.T., Canterford, L., Hoke, D., Williamson, N.A., McLean, C.A., Masters, C.L., and 1. 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 γ-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, 8359-8368. 6. Greenough, 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, 9776-86.

Biosensis是一家由生命科学家和商业团队组成的公司,致力于为全球学术界和工业界的研究人员提供支持。该团队在基础和应用生命科学研究方面拥有超过100年的经验,并在生命科学研究和诊断市场的生命科学抗体,试剂和试剂盒的商业化方面拥有50多年的经验。

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