製品名
スペクトリン ヒト赤血球由来, buffered aqueous glycerol solution
biological source
human erythrocytes
form
buffered aqueous glycerol solution
UniProt accession no.
application(s)
cell analysis
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... SPTA1(6708)
Analysis Note
高純度
General description
スペクトリンは、脊椎動物の真核細胞膜表面を覆っているタンパク質ネットワークの主要な構成要素です。2つのサブユニット(約230 kDaと250 kDa)からなる、高分子量のヘテロ二量体です。スペクトリンは長さ約200～260 nm、直径3～6 nmのひも状の柔軟性高分子で、両末端にアクチン結合ドメインを有しています。αサブユニットとβサブユニットから構成され、これらはいずれもa-アクチニンに関係しています。このαとβサブユニットは横方向に会合し、逆平行のヘテロ二量体を形成しています。このヘテロ二量体はさらに頭部同士で会合してヘテロ用量体を形成します。5～7個のひも状スペクトリン分子が多角形のネットワークを形成し、長さ約40 nmの短いアクチン線維につながって、赤血球膜の骨格が構築されています。赤血球のこのスペクトリン-アクチンネットワークは、主にスペクトリンとアンキリンの会合によって膜の二重層に結合し、さらにアニオン交換輸送体の細胞質ドメインに結合しています。赤血球におけるスペクトリン骨格の主な機能は、膜の二重層の機械的支持体となり、循環血中の細胞の生存を助けることです。
The C-terminus of spectrin contains a calmodulin-like EF domain. This domain is critical for binding of spectrin to actin for proper cytoskeletal formation. Deletion of this domain results in weak, irregularly-shaped red blood cells.
Physical form
100 mM塩化ナトリウム、10 mMリン酸バッファ-(pH 8.0)、1 mMジチオスレイト-ル、1mM EDTAおよび0.1 mMフェニルメチルスルホニルフルオライドを含有する50%グリセロ-ル溶液
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
保管分類
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Matthew N Rasband
Current biology : CB, 23(5), R197-R198 (2013-03-12)
Axons must be supported by a strong and flexible cytoskeleton. New 'super-resolution' imaging of the submembranous axonal cytoskeleton reveals that it is organized in a periodic, ladder-like structure with alternating rings of actin linked together by intervening complexes of spectrin.
Matthew D Vesely et al.
Annals of the New York Academy of Sciences, 1284, 1-5 (2013-05-09)
Accumulated data from animal models and human cancer patients strongly support the concept that the immune system can identify and control nascent tumor cells in a process called cancer immunosurveillance. In addition, the immune system can also promote tumor progression
Alessandro Borgia et al.
Nature communications, 3, 1195-1195 (2012-11-15)
Theory, simulations and experimental results have suggested an important role of internal friction in the kinetics of protein folding. Recent experiments on spectrin domains provided the first evidence for a pronounced contribution of internal friction in proteins that fold on
Pan Zhang et al.
Nucleic acids research, 41(10), 5321-5340 (2013-04-11)
Telomere integrity is critical for telomere function and genomic stability. We previously demonstrated that non-erythroid α-spectrin (αIISp) is present in mammalian cell nuclei where it is important in repair of DNA interstrand cross-links (ICLs) and chromosome stability. We now demonstrate
Laura Picas et al.
ACS nano, 7(2), 1054-1063 (2013-01-26)
The erythrocyte membrane, a metabolically regulated active structure that comprises lipid molecules, junctional complexes, and the spectrin network, enables the cell to undergo large passive deformations when passing through the microvascular system. Here we use atomic force microscopy (AFM) imaging
関連コンテンツ
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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