产品名称
Tau-381 human, recombinant, expressed in E. coli, ≥90% (SDS-PAGE), lyophilized powder
biological source
human
recombinant
expressed in E. coli
assay
≥90% (SDS-PAGE)
form
lyophilized powder
mol wt
39.7 kDa
UniProt accession no.
application(s)
cell analysis
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... MAPT(4137)
Biochem/physiol Actions
Isoform of Tau, variant 1N3R, having 3 microtubule binding repeats (R) and one amino terminal insert (N).
Microtubule associated protein tau (MAPT) aids in the assembly and maintenance of microtubule structure. Loss of expression of MAPT results in developmental delay and learning disability. The protein has been associated with pathology of Alzheimer′s disease (AD).
General description
The gene microtubule associated protein tau (MAPT) is localized on human chromosome 17q21.3. It is expressed in neurons, more specifically in axons.
Preparation Note
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.
wgk
WGK 1
存储类别
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Microdeletion encompassing MAPT at chromosome 17q21. 3 is associated with developmental delay and learning disability
Shaw-Smith, Charles, et al
Nature Genetics (2006)
The H1c haplotype at the MAPT locus is associated with Alzheimer's disease
A.J. Myers
Human Molecular Genetics (2005)
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
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
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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