Our broad portfolio consists of multiplex panels that allow you to choose, within the panel, analytes that best meet your needs. On a separate tab you can choose the premixed cytokine format or a single plex kit.
Cell Signaling Kits & MAPmates™
Choose fixed kits that allow you to explore entire pathways or processes. Or design your own kits by choosing single plex MAPmates™, following the provided guidelines.
The following MAPmates™ should not be plexed together: -MAPmates™ that require a different assay buffer -Phospho-specific and total MAPmate™ pairs, e.g. total GSK3β and GSK3β (Ser 9) -PanTyr and site-specific MAPmates™, e.g. Phospho-EGF Receptor and phospho-STAT1 (Tyr701) -More than 1 phospho-MAPmate™ for a single target (Akt, STAT3) -GAPDH and β-Tubulin cannot be plexed with kits or MAPmates™ containing panTyr
.
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Select A Species, Panel Type, Kit or Sample Type
To begin designing your MILLIPLEX® MAP kit select a species, a panel type or kit of interest.
Custom Premix Selecting "Custom Premix" option means that all of the beads you have chosen will be premixed in manufacturing before the kit is sent to you.
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96-Well Plate
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Add Additional Reagents (Buffer and Detection Kit is required for use with MAPmates)
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
Space Saver Option Customers purchasing multiple kits may choose to save storage space by eliminating the kit packaging and receiving their multiplex assay components in plastic bags for more compact storage.
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Neurodegenerative diseases are characterized by deterioration of neurons or their myelin sheath, disrupting transmission of sensory information, movement control and more. Because these cells are not easily regenerated, buildup of amyloid plaques can lead to disorders such as Alzheimer’s and Parkinson’s disease, and non-amyloid-related degeneration can cause ALS and MS.
Calbiochem® provides high quality small molecules inhibitors for elucidating the pathogenesis of both amyloid- and non-amyloid-related neurodegeneration, which have been cited in numerous peer-reviewed publications.
Aβ (β-amyloid peptide) is a major component of neuritic plaques and cerebrovascular amyloid deposits in the brains of patients with Alzheimer’s disease (AD). A long-standing hypothesis has been that Aβ deposits are neurotoxic and are causative factors in the development and progression of AD. Hence, development of inhibitors of Aβ fibrillogenesis has become an important area of research ...
A large number of autonomic neurons are cholinergic in nature. Cholinergic terminals contain a large number of small acetylcholine (ACh)-containing, membrane-bound vesicles concentrated near the synaptic end. Following their release from the pre-synaptic end, ACh molecules activate cholinoreceptors on the post-synaptic membrane. Acetylcholinesterase (AChE) is a tetrameric protein that catalyzes the hydrolysis of acetylcholine. AChE inhibitors, which increase the availability of acetylcholine in central synapses, as well as muscarinic agonists, have become the main approach to symptomatic treatment of patients with Alzheimer's disease ...
Monoamine Oxygenase (MAO) Inhibitors act by inhibiting the activity of monoamine oxidase, thus preventing the breakdown of monoamine neurotransmitters and thereby increasing their availability.
Deposition of Aβ is an early event in the pathogenesis of Alzheimer's disease (AD). The β-amyloid gene, located on chromosome 21, encodes a transmembrane amyloid precursor protein (APP), which gives rise to Aβ. Cleavage of APP by β-secretase and γ-secretases represents the amyloidogenic pathway for processing of APP. The characterization of APP secretases during the past few years has provided significant advancement in therapeutic strategies that may lead to limiting the build-up of Aβ peptide in the brain and eliminate or delay the pathological effects of AD ...
Tau protein aggregation is a hallmark of Alzheimer’s and other degenerative diseases. Aggregation of tau in the neurons is to be toxic to the cells. Tau Aggregation Inhibitors act by hindering this neuronal cell dysfunction.