S3644
Spectrin from human erythrocytes
buffered aqueous glycerol solution
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About This Item
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Source biologique
human erythrocytes
Niveau de qualité
Forme
buffered aqueous glycerol solution
Numéro d'accès UniProt
Application(s)
cell analysis
Conditions d'expédition
wet ice
Température de stockage
−20°C
Informations sur le gène
human ... SPTA1(6708)
Description générale
Spectrin is the major component of the protein network, which covers the cytoplasmic surface of vertebrate erythrocyte membranes. It is a high molecular weight heterodimer composed of two subunits (molecular weights of approximately 230 kDa and 250 kDa). Spectrins are extended flexible molecules approximately 200-260 nm in length and 3-6 nm across with actin-binding domains at each end. Spectrins are composed of α and β subunits, which are both related to a-actinin. The α and β subunits associate laterally to form antiparallel heterodimers and the heterodimers are assembled head-head to form heterotetramers. The erythrocyte membrane skeleton is organized as a polygonal network formed by five to seven extended spectrin molecules linked to short actin filaments approximately 40 nm in length. The spectrin-actin network of erythrocytes is coupled to the membrane bilayer primarily through the association of spectrin with ankyrin, which in turn is bound to the cytoplasmic domain of the anion exchanger. A major function of the spectrin skeleton in erythrocytes is to provide mechanical support for the membrane bilayer and allow survival of the cells in circulation.
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.
Qualité
Highly purified
Forme physique
Solution in 50% glycerol containing 100 mM sodium chloride, 10 mM phosphate buffer, pH 8.0, 1 mM dithiothreitol, 1mM EDTA and 0.1 mM phenylmethylsulfonyl fluoride.
Clause de non-responsabilité
Ce produit, destiné à la recherche scientifique, est soumis à une réglementation spécifique en France, y compris pour les activités d′importation et d′exportation (Article L 1211-1 alinéa 2 du Code de la Santé Publique). L′acheteur (c′est-à-dire l′utilisateur FINAL) est tenu d′obtenir une autorisation d′importation auprès du ministère français de la recherche, mentionné à l′article L1245-5-1 II du Code de la Santé Publique. En commandant ce produit, vous confirmez détenir l′autorisation d′importation requise.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Peter Bellstedt et al.
Journal of biomolecular NMR, 54(4), 325-335 (2012-11-28)
We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically
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
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
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