MW 426.1 Da, Purity >99%. Selective neural Wiskott-Aldrich syndrome protein (N-WASP) inhibitor. Binds the GTPase binding domain stabilising the autoinhibited conformation. Prevents activation of Arp2/3 complex in the actin cytoskeleton.
AI413597, AW045860, DDPAC, FLJ31424, FTDP 17, G protein beta1/gamma2 subunit interacting factor 1, MAPT, MAPTL, MGC134287, MGC138549, MGC156663, MGC2124, MGC60244, MSTD, MTBT1, MTBT2, Microtubule associated protein tau isoform 4, Microtubule-associated protein tau, Mtapt, Neurofibrillary tangle protein, PHF-tau, PPND, PPP1R103, Paired helical filament-tau, Protein phosphatase 1, regulatory subunit 103, RGP 4, RGS4_HUMAN, RNPTAU, Regulator of G protein signalling 4, Regulator of G-protein signaling 4, SCZD 9, Schizophrenia disorder 9, TAU_HUMAN, Tauopathy and respiratory failure, Tauopathy and respiratory failure, included, pTau
MW 426.1 Da, Purity >99%. Selective neural Wiskott-Aldrich syndrome protein (N-WASP) inhibitor. Binds the GTPase binding domain stabilising the autoinhibited conformation. Prevents activation of Arp2/3 complex in the actin cytoskeleton.
Soluble in DMSO to 100 mM.
Selective neural Wiskott-Aldrich syndrome protein (N-WASP) inhibitor. Binds the GTPase binding domain stabilising the autoinhibited conformation. Prevents activation of Arp2/3 complex in the actin cytoskeleton.
Tau also known as MAPT (Microtubule-Associated Protein Tau) is a protein that primarily functions in stabilizing microtubules. It plays an essential role in ensuring proper neuronal cell shape and intracellular transport. Tau has several isoforms generated through alternate splicing each with a specific mass ranging from 45 to 68 kDa. This protein is abundantly found in neurons within the central nervous system although its presence has also been detected in other cell types but at much lower levels.
Tau acts to stabilize microtubules which are structural components critical for maintaining neuronal morphology and function. It may also interact with actin filaments and other cytoskeletal proteins. Tau’s stabilization of microtubules is important for axonal transport a process that delivers essential nutrients and signaling molecules across cells. tau is often associated with complexes involving cytoskeletal elements and various microtubule-associated proteins.
The role of Tau plays in cellular signaling and transport makes it an important component of pathways like the MAPK/ERK pathway and PI3K/AKT signaling. These pathways are involved in cell differentiation survival and proliferation. Other notable proteins that share these pathways include amyloid precursor protein (APP) and glycogen synthase kinase 3 beta (GSK-3β). Tau's hyperphosphorylation can disrupt these pathways adversely affecting neuronal health.
The aggregation and malfunction of Tau are intensely linked to Alzheimer's disease and frontotemporal dementia. Abnormal phosphorylation of Tau leads to the formation of neurofibrillary tangles a hallmark of Alzheimer's pathology. In these conditions Tau interacts with proteins such as amyloid-beta (Aβ) found in amyloid plaques. These pathologies highlight Tau’s role not just as a structural protein but as a critical factor in neurodegenerative processes.
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2D chemical structure image of ab141085, Wiskostatin, N-WASP inhibitor
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