Presenilin 1 (PS-1, PS1, PSEN1) ELISA Kit (Part No. PS1-ELISA, 96T)

Presenilin 1 (PS-1, PS1, PSEN1) ELISA Kits

High Sensitivity

Separate kits are available for human, mouse, rat, canine and rabbit specific Presenilin 1. Use available options menu to order.

Part No. PS-1 ELISA. Lead time: Approximately 4 weeks.

Highly sensitive pg/ml colorimetric detection in Sandwich ELISA strip plate format.
Affinity purified polyclonal antibody capture antibody on plate. Separate HRP-conjugated detection antibody.
Rapid detection. 30 min total incubation at 37^oC.
Suitable for membrane extracts, cell lysates, tissue extracts
Separate kits are available for human, rat, mouse, canine and rabbit

View General Protocol

*(Use the protcol shipped with the kit for your experiment).

Specifications: Presenilin 1 ELISA Kits

Species	Standard Peptide	Assay Range
Human	900 pg/ml	10 - 700 pg/ml
Rat	72 pg/ml	2 - 55 pg/ml
Mouse	72 pg/ml	2 - 55 ng/ml
Canine	90 pg/ml	2 - 80 pg/ml
Rabbit	90pg/ml	2 - 80 pg/ml

Use Available Options menu to select species specificity of the Presenilin 1 ELISA Kits

Overview:

Presenilins (Presenilin 1 and Presenilin 2) are multipass-integral membrane proteins thought to function as the catalytic subunit of the gamma-secretase complex, a protease complex that catalyzes the cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Presenilins also cleave E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin and negatively regulating Wnt signaling.

The gamma-secretase complex is composed of presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2, and additional proteins. These proteins are sufficient for catalytic activity. Other components associated with the gamma-secretase complex include SLC25A64, SLC5A7, and PHB. Presenilin 1 is located in the endoplasmic reticulum membrane, Golgi membrane and cell surface membrane. Presenilin-1 is expressed in a wide range of tissues that include brain, liver, spleen and lymph nodes.

Icon Image: Solution structure of Presenilin 1 of amino acids 292-497.

DOI:10.2210/pdb2kr6/pdb

Price (USD)	No. of Kits	Number of Assays
$635	1	96T

Select species in available options menu.

Methods Overview:

The provided ELISA 96-well micro-strip plate is coated with an affinity purified antibody selective to the antigen. Upon addition of samples to the wells, the antigen in solution binds to the antibody bound to the plate. A second affinity purified antibody bound in a complex with horse-radish peroxidase (HRP) is then added, followed by a 30 min incubation period at 37^oC. Unbound antibody is washed away, and then color reagents are added, which upon conversion by HRP, become blue colored. A stop solution is then added, converting the solution to yellow. An absorbance multiplate reader is used to quantitate the colorimetric reaction at 450 nm.

This ELISA assay kit provides a standard peptide solution with known concentration to calibrate absorbance readings to concentration.

Image: Structure of Apo E revealing allelic variants. Source PDB:

DOI:10.2210/pdb1le2/pdb

Representative Sandwich ELISA Methods

Steps of Sandwich ELISA
1. Add sample

3. Add HRP-Antibody mixture, incubate 30 min at 37^oC

4. Add the color reagents

5. Add the stop solution

References on Presenilin 1

Ankarcrona, M., & Hultenby, K. (2002). Presenilin-1 is located in rat mitochondria. Biochemical and Biophysical Research Communications, 295(3), 766-770. Crump, C. J., Fish, B. A., Castro, S. V., Chau, D.-M., Gertsik, N., Ahn, K., Stiff, C., et al. (2011). Piperidine acetic acid based γ-secretase modulators directly bind to Presenilin-1. ACS chemical neuroscience, 2(12), 705-710.
De Gasperi, R., Sosa, M. A. G., Dracheva, S., & Elder, G. A. (2010). Presenilin-1 regulates induction of hypoxia inducible factor-1α: altered activation by a mutation associated with familial Alzheimer’s disease. Molecular neurodegeneration, 5(1), 38. BioMed Central Ltd.
Doan, A., Thinakaran, G., Borchelt, D. R., Slunt, H. H., Ratovitsky, T., Podlisny, M., Selkoe, D. J., et al. (1996). Protein topology of presenilin 1. Neuron, 17(5), 1023-1030.
Kandimalla, R. J., Wani, W. Y., Bk, B., & Gill, K. D. (2012). siRNA against presenilin 1 (PS1) down regulates amyloid beta 42 production in IMR-32 cells. Journal of biomedical science, 19(1), 2.
Koizumi, K., Nakajima, M., Yuasa, S., Saga, Y., Sakai, T., Kuriyama, T., Shirasawa, T., et al. (2001). The role of presenilin 1 during somite segmentation. Development Cambridge England, 128(8), 1391-1402.
Refolo, L. M., Eckman, C., Sanders, S., Yager, D., Perez-tur, J., Younkin, S., et al. (1998). Presenilin 1 Mutations. Human Molecular Genetics, 42(43), 256-258.

For research only. Not for diagnostics.

Safety: Stop solution contains acid. Avoid ingestion, skin and eye contact.

Storage: 4^oC.

Shipping. Overnight domestic delivery recommended. Also available for international delivery; please inquire for shipping cost.

Category	Download Link
Protocol Manual	click here
MSDS	click here

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