抗Tau [TAU 2]抗体 | Anti-Tau [TAU 2] antibody

• 特長
• 価格
• 製品情報
• APPLICATION
• PROPERTIES
• TARGET

特長

• 高品質の抗体です。
• 幅広い研究分野に関連する抗体を取り揃えています。
• 使用されたアプリケーションや動物種などの情報が充実しています。
• 多数の論文で使用実績がある信頼性の高い抗体です。

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価格

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製品情報

Host	Mouse
Clonality	Monoclonal
Clone Name	TAU 2
Isotype	IgG1
Application	WB
Reactivity	Human, Bovine

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APPLICATION

Application Note

For IHC-P: Use at an assay dependent dilution. For WB: Use at a concentration of 1-2 μg/ml. Optimal dilutions/concentrations should be determined by the researcher.

Calculated MW	79 kDa. ( Note )
Specificity/Sensitivity	GTX12356 stains the human neurofibrillary tangles, neuropil threads and neuritic plaques associated with Alzheimer's disease. The antibody also stains astrocytes and ribosomes. Tau-2 may be used with formalin-fixed paraffin-embedded sections of human brain tissue.

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PROPERTIES

Form	Liquid
Buffer	Phosphate-buffered saline, pH 7.4, and 150 mM NaCl containing 0.09% sodium azide and 1% BSA
Storage	Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration	0.1 mg/ml (Please refer to the vial label for the specific concentration.)
Immunogen	Recombinant full length protein
Purification	Protein A/G purified
Conjugation	Unconjugated
Note	For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.

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TARGET

Synonyms	Microtubule Associated Protein Tau , Ddpac , Ftdp-17 , Maptl , Mstd , Mtbt1 , Mtbt2 , Ppnd , Ppp1R103 , Tau , Mapt
Background	Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. 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). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.
Database	・ Gene ID: 4137 ・ UniProt: P10636

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