S3644
Spectrin from human erythrocytes
buffered aqueous glycerol solution
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About This Item
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biological source
human erythrocytes
Quality Level
form
buffered aqueous glycerol solution
UniProt accession no.
application(s)
cell analysis
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... SPTA1(6708)
General description
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.
Quality
Highly purified
Physical form
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.
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.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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
S L Shammas et al.
Biophysical journal, 103(10), 2203-2214 (2012-12-04)
Many intrinsically disordered proteins (IDPs) are significantly unstructured under physiological conditions. A number of these IDPs have been shown to undergo coupled folding and binding reactions whereby they can gain structure upon association with an appropriate partner protein. In general
Meng He et al.
The Journal of biological chemistry, 287(52), 43995-44005 (2012-11-07)
Ankyrin-G (AnkG) coordinates protein composition of diverse membrane domains, including epithelial lateral membranes and neuronal axon initial segments. However, how AnkG itself localizes to these membrane domains is not understood. We report that AnkG remains on the plasma membrane in
Makoto Ishihara et al.
Blood, 121(21), 4340-4347 (2013-03-30)
Adult T-cell leukemia (ATL) is one of the most aggressive hematologic malignancies caused by human T-lymphotropic virus type 1 (HTLV-1) infection. The prognosis of ATL is extremely poor; however, effective strategies for diagnosis and treatment have not been established. To
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