Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to
worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting
immunostaining in relation to complex human pathologies.
Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding.
Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".
(tested or 100% immunogen sequence identity)
IHC - Paraffin (1:300)
IHC - Frozen (1:1000)
Performing IHC? See our complete line of Immunohistochemistry Reagents including antigen retrieval solutions, blocking agents
ABC Detection Kits and polymers, biotinylated secondary antibodies, substrates and more.
Synthetic peptide corresponding to amino acids 31-47 of Presenilin-2.
Recognizes human presenilin-2 (PSEN2), binding to neurons in both normal and Alzheimer's disease brain. Mutation of PSEN2 is associated with the early onset form of autosomal dominant Alzheimer's disease. PSEN2 is an essential component of the gamma-secretase complex along with APH-1 (APH-1A or APH-1B), PSEN1, Pen-2 (PEN2), and nicastrin (NCSTN). This endoprotease complex plays a vital role in the evolutionarily conserved Notch signaling pathway, by catalyzing the intramembrane S3 cleavage of ligand-activated Notch receptor proteins (Notch1-4), resulting in the generation and release of an activated NICD fragment, which then translocates to the nucleus and activates the transcription of downstream effector genes.
Immunohistology: This product does not require protein digestion pre-treatment of paraffin sections. This product does not require antigen retrieval using heat treatment prior to staining of paraffin sections.
Alzheimer's disease (AD) patients with an inherited form of the disease carry mutations in the presenilin proteins (PSEN1 or PSEN2) or the amyloid precursor protein (APP). These disease-linked mutations result in increased production of the longer form of amyloid-beta (main component of amyloid deposits found in AD brains). Presenilins are postulated to regulate APP processing through their effects on gamma-secretase, an enzyme that cleaves APP.