MAPT Human 383a.a.
Description
MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.
Product Science Overview
Microtubule-Associated Protein Tau (MAPT), commonly referred to as Tau protein, is a critical component in the stabilization and assembly of microtubules in neuronal cells. The specific variant, Tau 383 a.a., is a human recombinant protein consisting of 383 amino acids. This variant is often used in research to understand its role in neurodegenerative diseases, particularly Alzheimer’s disease.
Tau protein exists in several isoforms, which are produced through alternative splicing of the MAPT gene. The Tau 383 a.a. variant, also known as 0N4R, lacks N-terminal inserts and contains four microtubule-binding repeats . This structure allows it to interact effectively with microtubules, promoting their stability and assembly .
Tau proteins are primarily found in neurons, where they bind to microtubules and promote their assembly and stability. This function is crucial for maintaining the structure and function of axons. The Tau 383 a.a. variant is particularly important in research due to its involvement in the formation of neurofibrillary tangles, a hallmark of Alzheimer’s disease .
In neurodegenerative diseases like Alzheimer’s, Tau proteins become hyperphosphorylated, leading to their detachment from microtubules and subsequent aggregation into paired helical filaments and neurofibrillary tangles . These aggregates disrupt neuronal function and contribute to cell death. Studying the Tau 383 a.a. variant helps researchers understand the mechanisms behind these pathological changes and develop potential therapeutic interventions.
Recombinant Tau 383 a.a. is widely used in various research applications, including:
