Human phosphorylated Tau181 Protein
Catalog# HA211530
Human phosphorylated Tau181 Protein
Product Information
Product name
Human phosphorylated Tau181 Protein
Catalog No.
HA211530
Accession
P10636-8
Protein construction
Tau/Tau 441 (1-441)-pT181
Source
HEK293
Bio Activity
Testing in progress.
Purity
>95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU per μg by the LAL method.
Formulation
Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4, 5% Trehalose, 5% mannitol.
Species
Human
Background
Tau, also known as MAPT (microtubule-associated protein tau), MAPTL, MTBT1 or TAU, is a 758 amino acid protein that localizes to the cytoplasm, as well as to the cytoskeleton and the cell membrane, and contains four Tau/MAP repeats. Expressed in neuronal tissue and existing as multiple alternatively spliced isoforms, Tau functions to promote microtubule assembly and stability and is thought to be involved in the maintenance of neuronal polarity. Tau may also link microtubules with neural plasma membrane components and, addition to its role in microtubule stability, is also necessary for cytoskeletal plasticity. Tau is highly subject to a variety of post-translational modifications, including phosphorylation on serine and threonine residues, polyubiquitination (and subsequent proteasomal degradation) and glycation of specific Tau isoforms. Defects in the gene encoding Tau are associated with Alzheimers disease, pallido-ponto-nigral degeneration (PPND), corticobasal degeneration (CBD) and progressive supranuclear palsy (PSP).
Usage guide
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped with blue ice. Bulk packages of recombinant proteins are provided as frozen liquid which are shipped with dry ice.
Storage
Please avoid repeated freeze-thaw cycles. Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ It is recommended that aliquot the reconstituted solution to minimize freeze-thaw cycles.
Reconstitution
Reconstitute at 250 μg/ml in sterile water.
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