Abcam, ab315045, Human Prion protein PrP ELISA Kit

Size: 1 x 96Tests
Human Prion protein PrP ELISA Kit is a single-wash 90-min Simplestep used to quantify Human Prion protein PrP with a sensitivity of 19.817 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader - Validated on a number of sample types including cerebrospinal fluid (CSF) - Design your own immunoassay: we also offer the conjugation-ready antibody pair
Key facts
Detection method:Colorimetric,
Sample types:Serum, Heparin Plasma, EDTA Plasma, Citrate plasma, Cerebral Spinal Fluid,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 19.817 pg/mL,
Range:59.375 - 3800 pg/mL,
Assay time:1h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
Human Prion protein PrP SimpleStep ELISA® kit is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Prion protein PrP protein in Serum, EDTA Plasma, Cit Plasma, Hep Plasma, Cerebral Spinal Fluid. Quantitate Human Prion protein PrP with 19.817 pg/ml sensitivity.
SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:
-Single-wash protocol reduces assay time to 90 minutes or less
-High sensitivity, specificity and reproducibility from superior antibodies
-Fully validated in biological samples
-96-wells plate breakable into 12 x 8 wells strips
A 384-well SimpleStep ELISA® microplate (
ab203359
) is available to use as an alternative to the 96-well microplate provided with SimpleStep ELISA® kits.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Prion protein also known as PrP or major prion protein plays a mechanical role in the normal functioning of brain cells. It is a glycoprotein with a flexible structure and has an approximate mass of 35-36 kDa. PrP expression is high in nervous tissue. It is present in neurons and glial cells but also surfaces in other tissues like heart and kidney. Alternate names like p-pr-p and f89 refer to specific conformations or studies related to its structure.
Biological function summary
Prion protein assists in maintaining normal cell activities. Researchers do not fully understand its exact biological role but it might be involved in copper ion uptake and protection against oxidative stress. PrP can form complexes with other cellular proteins some of which help in routing signals inside the cell. Additionally prion protein may have synaptic functions related to neurodevelopment and neuroprotection.
Pathways
Prion protein links to both neuroprotective and neurodegenerative pathways. It participates in signaling pathways that protect neurons from apoptosis. This protein associates closely with copper-dependent pathways possibly related to its capacity to bind copper ions which affects oxidative stress responses. Prion protein also interacts with proteins like synapsin to modulate synaptic transmission.
Prion protein is directly related to prion diseases such as Creutzfeldt-Jakob disease and kuru. These diseases arise from misfolded forms of PrP which aggregate and cause neurodegeneration. The misfolded form referred to as PrP^Sc can induce normal PrP to misfold propagating disease. Dopamine receptor proteins and synaptic proteins can indirectly interact or be affected in these disorders highlighting a complex network of affected neural functions.