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T9825

Sigma-Aldrich

Tau-383 human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), lyophilized powder

Synonym(s):

MAPTL, MTBT1, TAU

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About This Item

MDL number:
MFCD07785732
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

Quality Level

200

recombinant

expressed in E. coli

Assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

40 kDa

technique(s)

western blot: suitable

suitability

suitable for Western blot

UniProt accession no.

P10636

application(s)

cell analysis

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... MAPT(4137)

General description

Research area: Neuroscience

Tau-383 belongs to the neuronal microtubule-associated protein family and is found in the axons of the CNS (central nervous system). It is encoded by the MAPT (microtubule associated protein tau) gene on chromosome 17q21 and exists in the form of 6 isoforms produced by the alternative splicing of m-RNA transcripts of MAPT (microtubule associated protein tau).

Application

The product can be utilized for systemic identification of Phosphorylation sites in microtubule-associated protein tau by using checkpoint kinases Chk1 and Chk2 in vitro.

Biochem/physiol Actions

Microtubule-associated protein tau is mainly involved in promoting the assembly and stability of microtubules in axons. The N terminal domain of tau protein is responsible for many important functions including regulation of microtubule dynamics, and spacing between microtubules and cell compartments. While the proline rich domain of the tau protein plays a key role in neuronal signaling, functioning, and maintenance of the cytoskeleton. The interaction between tau and the microtubules plays a crucial role in regulating cell signaling, synaptic plasticity, and genomic stability. Thus, an impaired interaction between Tau and microtubules leads to the development of several neurodegenerative diseases.
Isoform of Tau, variant 0N4R, having 4 microtubule binding repeats (R) and no amino terminal inserts (N)

Reconstitution

Lyophilized from MES, pH 6.8, containing NaCl and EGTA. When reconstituted in water to a protein concentration of 1 mg/mL, the resulting buffer will have ~50 mM MES, pH 6.8, 100 mM NaCl, and 0.5 mM EGTA.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

T9825-50UG:
T9825-50UG-PW:
T9825-VAR:
T9825-BULK:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Jhoana Mendoza et al.
Journal of proteome research, 12(6), 2654-2665 (2013-04-05)
Hyperphosphorylation of microtubule-associated protein tau is thought to contribute to Alzheimer's disease (AD) pathogenesis. We previously showed that DNA damage-activated cell cycle checkpoint kinases Chk1 and Chk2 phosphorylate tau at an AD-related site and enhance tau toxicity, suggesting potential roles
A Himmler et al.
Molecular and cellular biology, 9(4), 1381-1388 (1989-04-01)
Tau proteins consist of a family of proteins, heterogeneous in size, which associate with microtubules in vivo and are induced during neurite outgrowth. In humans, tau is one of the major components of the pathognomonic neurofibrillary tangles in Alzheimer's disease
Jesus Avila et al.
Physiological reviews, 84(2), 361-384 (2004-03-27)
The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal components such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated
M Goedert et al.
Neuron, 3(4), 519-526 (1989-10-01)
We have determined the sequences of isoforms of human tau protein, which differ from previously reported forms by insertions of 29 or 58 amino acids in the amino-terminal region. Complementary DNA cloning shows that the insertions occur in combination with

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