MAPT Human 412a.a.

Microtubule-Associated Protein Tau 412 a.a. Human Recombinant
Cat. No.
BT13219
Source
Escherichia Coli.
Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

MAPT Human Recombinant (Isoform 5) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 45.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Microtubule-associated protein tau (MAPT or Tau) is a protein that helps stabilize microtubules, which are important for cell structure and function. MAPT is primarily found in neurons of the central nervous system. When MAPT is defective and unable to stabilize microtubules properly, it can contribute to the development of neurodegenerative diseases like Alzheimer's disease.
Description
This product consists of the human MAPT protein, specifically isoform 5, produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain of 432 amino acids, with a His tag attached to the N-terminus for purification purposes. The molecular weight of the protein is 45.1 kDa, but it may appear larger on SDS-PAGE. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear and colorless solution that has been sterilized by filtration.
Formulation
The MAPT protein is supplied in a solution containing 0.5 mg/ml of protein, 20mM Tris-HCl buffer (pH 8.0), and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), keep the vial refrigerated at 4°C. For long-term storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA to a final concentration of 0.1% is recommended for long-term storage. Repeated freezing and thawing of the solution should be avoided.
Purity
The purity of the MAPT protein is greater than 80%, as determined by SDS-PAGE analysis.
Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Source
Escherichia Coli.
Amino Acid Sequence
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 PGGGKVQIIN KKLDLSNVQS KCGSKDNIKH VPGGGSVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.

Product Science Overview

Structure and Isoforms

Tau proteins are encoded by the MAPT gene and exist in several isoforms due to alternative splicing. The Tau 412 a.a. variant, also known as 1N4R, includes one amino terminal insert (N) and four microtubule-binding repeats ® . This isoform lacks a projection domain region, which is present in other Tau isoforms .

Expression and Purification

The recombinant Tau 412 a.a. protein is typically expressed in Escherichia coli (E. coli) and purified to a high degree of purity, often exceeding 90% . This high purity makes it suitable for various biochemical applications, including SDS-PAGE and Western Blotting .

Function and Significance

Tau proteins are essential for promoting microtubule assembly and stability. They bind to microtubules through their C-terminal region, while the N-terminal region interacts with neural plasma membrane components . This dual binding suggests that Tau functions as a linker protein, contributing to the establishment and maintenance of neuronal polarity .

Pathological Implications

Abnormal phosphorylation of Tau proteins can lead to their detachment from microtubules, resulting in microtubule disassembly. This process is implicated in several neurodegenerative diseases, including Alzheimer’s disease, where hyperphosphorylated Tau forms neurofibrillary tangles .

Applications

Recombinant Tau 412 a.a. is widely used in research to study microtubule dynamics, Tau-related pathologies, and potential therapeutic interventions. Its ability to promote microtubule assembly and undergo hyperphosphorylation-induced self-assembly into filaments makes it a valuable tool in neurobiological studies .

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