T0451
Tau-410 human
recombinant, expressed in E. coli, ≥85% (SDS-PAGE), lyophilized powder
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About This Item
Productos recomendados
biological source
human
Quality Level
recombinant
expressed in E. coli
assay
≥85% (SDS-PAGE)
form
lyophilized powder
mol wt
42.6 kDa
UniProt accession no.
application(s)
cell analysis
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... MAPT(4137)
Biochem/physiol Actions
Isoform of Tau, variant 2N3R, having 3 microtubule binding repeats (R) and 2 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
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
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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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