| Catalogue No. |
R-1684-500 |
| Description |
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 detects all processed forms of Nicastrin. |
| Batch No. |
See vial label |
| Unit size |
500 ug |
| Antigen |
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. |
| Antibody Type |
Polyclonal |
| Produced in |
Rabbit |
| Applications |
WB and IP. Suggested concentration of 3-10 ug/mL is recommended for WB. Human or mouse brain samples commonly prepared with reducing (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. Unprocessed full length human Nicastrin is 709 amino acids, however this protein contains an N-terminal signal peptide which is considered to undergo cleavage during processing and transit to the cell plasma membrane, in addition the protein undergoes glycosylation to produce a glycoprotein of about 145 kDa apparent MW by SDS PAGE. Biosensis recommends that the optimal working dilution should be determined by the end user. |
| Specificity |
Confirmed by WB using peptide absorption. |
| Species Against |
Human, mouse, rat and guinea pig. Nicastrin is highly conserved, so cross-reactivity with other species is expected. |
| Form |
Lyophilized from PBS, pH 7.4. Contains no preservative. |
| Reconstitution |
Reconstitute in 500 uL of sterile water. Centrifuge to remove any insoluble material. |
| Storage |
Short term storage at 2-8C for one week. At -20C as an undiluted liquid for up to 12 months. |
| Expiry Date |
12 months after purchase |
| References |
1. 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.
2. 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.
3. 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. |
Images (click to zoom)
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Western Immunoblotting of mouse and human Nicastrin protein in mouse tissues and a human cell line (SHSY5Y). Membrane proteins were prepared and loaded as 20 µg protein per lane. |
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