Comparison

Presenilin 1 Elisa Kit (human, mouse, rat, canine)

Manufacturer Fivephoton
Category
Type Elisa-Kit
Specific against Human, Mouse, Rat, Canine
Amount 1 kit, 96T
Item no. PS1-ELISA
Targets PSEN1
eClass 6.1 32160605
eClass 9.0 32160605
Available
Poisonous Material
Sodium Azide (0.1%)
Highlights
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. 1 hr total incubation at 37C; 2 hr total incubation at RT
Suitable for membrane extracts, cell lysates, tissue extracts
Separate kits are available for human, rat, mouse, canine and rabbit
Background
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.
Description
Separate kits are available for human, mouse, rat, canine and rabbit specific Presenilin 1.
References
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 gamma-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-1alpha: 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.

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 1 kit, 96T
Available: In stock
available

Delivery expected until 6/6/2024 

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