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生物源
human
品質等級
重組細胞
expressed in E. coli
化驗
≥90% (SDS-PAGE)
形狀
lyophilized powder
分子量
39.7 kDa
UniProt登錄號
應用
cell analysis
運輸包裝
wet ice
儲存溫度
−20°C
基因資訊
human ... MAPT(4137)
一般說明
The gene microtubule associated protein tau (MAPT) is localized on human chromosome 17q21.3. It is expressed in neurons, more specifically in axons.
生化／生理作用
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).
Isoform of Tau, variant 1N3R, having 3 microtubule binding repeats (R) and one amino terminal insert (N).
重構
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.
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
The H1c haplotype at the MAPT locus is associated with Alzheimer's disease
A.J. Myers
Human Molecular Genetics (2005)
Microdeletion encompassing MAPT at chromosome 17q21. 3 is associated with developmental delay and learning disability
Shaw-Smith, Charles, et al
Nature Genetics (2006)
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
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
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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