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生物来源
human
质量水平
重组
expressed in E. coli
方案
≥90% (SDS-PAGE)
表单
lyophilized powder
分子量
39.7 kDa
UniProt登记号
应用
cell analysis
运输
wet ice
储存温度
−20°C
基因信息
human ... MAPT(4137)
一般描述
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
Isoform of Tau, variant 1N3R, having 3 microtubule binding repeats (R) and one amino terminal insert (N).
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).
重悬
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.
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
Microdeletion encompassing MAPT at chromosome 17q21. 3 is associated with developmental delay and learning disability
Shaw-Smith, Charles, et al
Nature Genetics (2006)
The H1c haplotype at the MAPT locus is associated with Alzheimer's disease
A.J. Myers
Human Molecular Genetics (2005)
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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