MAPT Human 381a.a.
Description
The MAPT is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY
KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L.
Product Science Overview
Microtubule-Associated Protein Tau (MAPT), commonly referred to as Tau, is a protein that plays a crucial role in stabilizing microtubules in neurons. The specific variant, Tau 381 a.a. (Human Recombinant), is a recombinant form of this protein, consisting of 381 amino acids. This article delves into the structure, function, and significance of this protein, particularly in the context of neurodegenerative diseases.
Tau proteins are encoded by the MAPT gene, which undergoes alternative splicing to produce six isoforms in the human brain. These isoforms vary in the number of microtubule-binding repeats and N-terminal inserts. Tau 381 a.a. is one of these isoforms, characterized by having three microtubule-binding repeats (3R) and one N-terminal insert (1N) .
The primary function of Tau is to stabilize microtubules, which are essential components of the cytoskeleton. Microtubules provide structural support and facilitate intracellular transport. Tau achieves this by binding to microtubules and promoting their assembly and stability . In its recombinant form, Tau 381 a.a. retains these functional properties, making it a valuable tool for research.
Tau is predominantly found in neurons of the central nervous system. When Tau proteins become hyperphosphorylated, they lose their ability to bind to microtubules effectively. This leads to the formation of neurofibrillary tangles, a hallmark of Alzheimer’s disease and other tauopathies . The accumulation of these tangles disrupts neuronal function and contributes to neurodegeneration.
Recombinant Tau 381 a.a. is produced using Escherichia coli (E. coli) expression systems. This recombinant protein is often used in research to study the biochemical properties of Tau, its interactions with other proteins, and its role in disease pathology . The recombinant form is typically purified to high levels of purity, ensuring its suitability for various experimental applications.
Recombinant Tau 381 a.a. is widely used in studies related to:
- Microtubule Dynamics: Understanding how Tau stabilizes microtubules and the effects of its dysfunction.
- Protein Interactions: Investigating how Tau interacts with other proteins and its role in cellular processes.
- Disease Mechanisms: Exploring the mechanisms underlying tauopathies and developing potential therapeutic interventions .
