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T9950

Tau-352 human

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

Synonim(y):

Human Tau Protein

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Gabaryty przesyłkiSKUDostępnośćCena netto
50 μg
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2710,00 zł

Informacje o tej pozycji

UNSPSC Code:
12352200
NACRES:
NA.32
MDL number:
Form:
lyophilized powder
Assay:
≥90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
36.8 kDa

2710,00 zł


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biological source

human

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

36.8 kDa

UniProt accession no.

application(s)

cell analysis

shipped in

wet ice

storage temp.

−20°C

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Ta pozycja
T9825T0326T7951
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

biological source

human

biological source

human

biological source

human

biological source

human

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

shipped in

wet ice

shipped in

wet ice

shipped in

dry ice

shipped in

dry ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

Application

Tau-352 human is a Tau isoform, variant 0N3R which means it consists of 3 microtubule binding repeats (R) and no amino terminal inserts (N). 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.[1]

Biochem/physiol Actions

Isoform of Tau, variant 0N3R, having 3 microtubule binding repeats (R) and no amino terminal inserts (N).
Tau-383 human belongs to neuronal microtubule-associated protein family that stimulates the microtubule assembly and stability as well as facilitates hyperphosphorylation-induced self-assembly into filaments.[2] Tau protein along with src can upregulate tyrosine kinase activity. Inhibition of Src kinase influences the action of tau on actin rearrangements which in turn impacts the growth-factor-induced actin remodeling.[3]

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.
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Klasa składowania

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
Vandana M Sharma et al.
Journal of cell science, 120(Pt 5), 748-757 (2007-02-08)
The microtubule-associated protein tau interacts with the SH3 domain of non-receptor Src family protein tyrosine kinases. A potential consequence of the SH3 interaction is the upregulation of tyrosine kinase activity. Here we investigated the activation of Src or Fyn by
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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SKUNUMER GTIN
T9950-50UG04061833385647

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