BioLegend 835201 Anti-Tau, 15-

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BioLegend 835201 Anti-Tau, 15-25
产品简介：
产品品牌：BioLegend
产品货号：835201
产品名称：BioLegend 835201 Anti-Tau, 15-25
产品规格：500 µL

产品说明：
Clone   TAU-13 (See other available formats)
Regulatory Status   RUO
Other Names
Microtubule-associated protein tau, PHF-tau, paired helical filament-tau, neurofibrillary tangle protein, microtubule-associated protein tau, isoform 4, G protein beta1/gamma2 subunit-interacting factor 1
Previously    Covance Catalog# MMS-520R
Isotype    Mouse IgG1, κ

描述
Tau蛋白是微管相关蛋白（MAP），其在中枢神经系统的神经元中大量存在，但在CNS星形胶质细胞、少突胶质细胞和其他地方也以非常低的水平表达。tau的主要功能之一是调节轴突微管的稳定性。Tau主要活跃于轴突的远端部分，提供微管稳定性和灵活性。神经系统的病理学和痴呆症，如阿尔茨海默氏症，其特征是tau蛋白已变得有缺陷，不再正确稳定微管。因此，tau形成具有特定结构性质的聚集体，称为成对螺旋丝（PHF），这是许多不同类型痴呆的特征，称为tau病。Tau有两种控制微管稳定性的主要方式：亚型和磷酸化。人类脑组织中存在六种tau亚型，它们通过结合结构域的数量来区分。三种异构体具有三个结合结构域，其余三种具有四个结合结构区。结合结构域位于蛋白质的羧基末端，带正电荷（用于与带负电荷的微管结合）。具有四个结合结构域的Tau亚型比具有三个结合结构区的Tau异构体更能稳定微管。因此，在人脑中，tau蛋白构成了一个由352-441个氨基酸组成的六种异构体家族。它们在N末端部分（外显子2和3）的29个氨基酸的零个、一个或两个插入，以及在C末端的三个或四个重复结合区方面也有所不同。因此，中枢神经系统中最长的同种型有四个重复序列（R1、R2、R3和R4）和两个插入物（总共441个氨基酸），而最短的同种型则有三个重复（R1、R3和C4）和没有插入物（共352个氨基酸）。Tau也是一种在最长的Tau亚型上具有79个潜在丝氨酸（Ser）和苏氨酸（Thr）磷酸化位点的磷蛋白。据报道，在正常tau蛋白中，大约有30个位点发生了磷酸化。在高度流行的散发性AD中，驱动tau损伤形成的机制尚不完全清楚，但似乎涉及影响tau功能、稳定性和聚集倾向的异常翻译后修饰（PTM）。
Tau proteins are microtubule-associated protein (MAPs) which are abundant in neurons of the central nervous system, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes and elsewhere. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is active primarily in the distal portions of axons providing microtubule stabilization as well as flexibility. Pathologies and dementias of the nervous system such as Alzheimer's disease feature tau proteins that have become defective and no longer stabilize microtubules properly. As a result, tau forms aggregates with specific structural properties referred to as Paired Helical Filaments (PHFs) that are a characteristic of many different types of dementias, known as tauopathies. Tau has two primary ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in human brain tissue, and they are distinguished by the number of binding domains. Three isoforms have three binding domains and the remaining three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (for binding to the negatively-charged microtubule). Tau isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They also differ in either zero, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-binding regions at the C-terminus. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). Tau is also a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. Phosphorylation has been reported on approximately 30 of these sites in normal tau proteins. Mechanisms that drive tau lesion formation in the highly prevalent sporadic form of AD are not fully understood, but appear to involve abnormal post-translational modifications (PTMs) that influence tau function, stability, and aggregation propensity.

Product Details
Verified Reactivity   Human
Antibody Type   Monoclonal
Host Species   Mouse
Preparation   Ascites
Concentration
The concentration is not quantified as this product is sold as undiluted crude mouse ascites fluid. The concentration might vary from lot-to-lot and an estimated concentration would be 1-3 mg/ml.

Storage & Handling
Store at -20°C or below. Upon initial thawing, apportion into working aliquots and store at -20°C or below. Avoid repeated freeze-thaw cycles to prevent denaturing the antibody. Do not store in frost-free freezers.

Application    WB - Quality tested
IHC-Other - Reported in the literature, not verified in house

Recommended Usage
Each lot of this antibody is quality control tested by western blotting. For western blotting, a dilution range of 1:500-1:1000 is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Antigen Details
Structure
Unmodified Tau isoforms have an apparent molecular weight ranging from 33-79 kD. Additional high and low molecular weight Tau species have been observed in brain tissues.

Distribution
Tissue distribution: Central nervous system, peripheral ganglia and nerves, kidney, skeletal, and heart muscle.
Cellular distribution: Cytoskeleton, nucleus, plasma membrane, and cytosol.

Function
Tau promotes microtubule assembly and stability. The short tau isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.

Interaction
Tau interacts with Sequestosome-1, Peptidyl-prolyl cis-trans isomerase FKBP4, casein kinase I isoform delta, serine/threonine-protein kinase Sgk1, Laforin, and alpha-synuclein.

Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family    Tau

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