Catalog NumberSizePrice (USD)Shopping Cart
MO20015100 ul$175.00Buy Now | Add to Cart
 
Type: Mouse IgG
 
Applications: IHC
E=ELISA; FACS; FC=Flow Cytometry; FPLC=Fast Protein Liquid Chromatography; GF=Gravity Flow; HPLC=High Performance Liquid Chromatography; ICC=Immunocytochemistry; IF=Immunofluorescence; IHC=Immunohistochemistry; IP=Immunoprecipitation; NAC=Non-adherent Cell Assays; NB=Neutralization of Bioactivity; SE=Sandwich ELISA; TPE=Targeted Protein Expression; WB=Western blotting; ; AC=Adherent Cell Assays; FM=Fluorescent Micsroscopy; ; ; BSC-CM5= Biacore Sensor Chip CM5; BSM=Biosactive Small Molecule or Peptide; CDM=Cell Differentiation Media; ; ; ; ; ; Health and Fitness; ; ; DNA Extraction/Purification; ; In vivo Like Assays
Species Reactivity: H
B=Bovine; Ca=Cat; Ch=Chicken; D=Dog; EQ=Equine; GP=Guinea Pig; H=Human; M=Mouse; P=Porcine; Pr=Primate; R=Rat; Rb=Rabbit; Y=Yeast; Xe=Xenopus; Ze=Zebrafish; ; ; ; NA-Not Applicable; STP=Step-Tactin Proteins; All
Format: Supernatant - liquid
 
Immunogen: Prokaryotic recombinant fusion protein corresponding to the extracellular protein of APP between the Kunitz protease inhibitor domain and the beta amyloid region.
 
Description/Data:
Picture

Alzheimer's disease, the most common cause of dementia in the elderly, exists in both familial and sporadic forms. Genetic studies have identified three genes; beta-amyloid precursor protein (APP),  Presenilin 1 and Presenilin 2 which, when mutated, can cause familial forms of Alzheimer's disease. APP and APP-like proteins are transmembrane glycoproteins with a similar modular domain structure.

APP-228 has been raised to the extracellular portion of APP between the Kunitz protease inhibitor domain and the beta amyloid region. This region shows the least homology with the APP-like proteins. APP-228 and does not cross-react with APP-like proteins.  APP reacts with large pyramidal cells as well as smaller neurons, astrocytes and microglia. APP 228 reacts with late-stage neurofibrillary tangle-bearing neurons, neuritic processes surrounding senile plaques and neuropil threads in gray matter of Alzheimer's disease brain. Unmasking in 1mM EDTA (pH8.0) in a pressure cooker may be required for up to 5 minutes in order for this APP-228 to work optimally.

Image: Human cortex, Alzheimer's disease: immunohistochemical staining using amyloid precursor protein-228. Note intense staining of neurofibrillary tangles and senile plaques. Paraffin section

APP228: Customer Publication

Picture[2]

A-Beta proteolysis by TTR is KPI-sensitive.
A- A-Beta incubated with TTR (A-Beta+TTR) shows a weaker A-Beta monomer band as compared to A-Beta alone (A-Beta), indicative of proteolysis, as analyzed by SDS-PAGE electrophoresis followed by western blot. Pre-incubation of TTR with pefabloc (A-Beta+(TTR+pefabloc)) and with an αAPP peptide containing the KPI domain (A-Beta+(TTR+KPI+−APP)) inhibits TTR proteolytic activity, whereas the αAPP peptide without the KPI domain (A-Beta+(TTR+KPI−−APP)) facilitates proteolysis. B- % of inhibition of TTR proteolysis by quantification of band intensity in A. C- Ultrastructural analysis by TEM of preparations incubated for 15 hours, as described in Materials and Methods. TTR inhibited A-Beta aggregation as compared with A-Beta incubated alone (upper panels). Pre-incubation of TTR with αAPP peptide containing the KPI domain (A-Beta+(TTR+KPI+−APP)) abrogated TTR ability to avoid A-Beta aggregation, whereas αAPP lacking the KPI domain (A-Beta+(TTR+KPI−−APP)) did not affected TTR activity (lower panels). Scale bar=500 nm. PLoS ONE. 2008; 3(8): e2899. Published online 2008 August 6. doi: 10.1371/journal.pone.0002899.