S1515
Anti-Spectrin antibody produced in rabbit
whole antiserum
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Synonym(s):
Anti-EL2, Anti-HPP, Anti-HS3, Anti-SPH3, Anti-SPTA
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
whole antiserum
antibody product type
primary antibodies
clone
polyclonal
contains
15 mM sodium azide
species reactivity
human
technique(s)
western blot: 1:400
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SPTA1(6708) , SPTB(6710) , SPTBN1(6711) , SPTBN2(6712) , SPTBN4(57731) , SPTBN5(51332)
Related Categories
General description
Spectrin is a multifunctional protein that has lipid-binding sites within CH (calponin-homology) tandem domains, a PH (pleckstrin homology) domain and triple helical segments. It is located on chromosome 1q23.1.
Spectrin is the major cytoskeletal component in erythrocytes. It is composed of two types of polypeptides known as α and β with molecular weights of 240 and 220 kDa, respectively. The α- and β-chains form heterotetramers which are linked end-to-end via oligomeric actin and band 4.1 protein.
Specificity
The antibody reacts specifically with the α and β chains of human erythrocyte spectrin.
Immunogen
spectrin from freshly prepared human erythrocyte ghosts.
Application
Anti-Spectrin antibody has been used in western blotting immunofluorescence and immunostaining.
Biochem/physiol Actions
Spectrins modulates the cell morphology and mechanical properties. Spectrins also participates in the cell cycle by controlling the upregulation of membrane receptors. α- and β spectrins are essential for the development of nervous system.
The spectrin-based membrane skeleton is essential to provide mechanical stability and membrane integrity. It is also responsible for protein organization, trafficking and resilience of erythrocytes.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Natalie J Spillman et al.
Cellular microbiology, 19(6) (2017-01-10)
The malaria parasite exports numerous proteins into its host red blood cell (RBC). The trafficking of these exported effectors is complex. Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite.
Physiologically important secondary modifications of red cell membrane in hereditary spherocytosis-evidence for in vivo oxidation and lipid rafts protein variations
Margetis P, et al.
Blood Cells, Molecules and Diseases, 38(3), 210-220 (2007)
Spectrin and phospholipids - the current picture of their fascinating interplay.
Boguslawska DM, et al.
Cellular & Molecular Biology Letters, 19(1), 158-179 (2014)
A Choudhury et al.
Parasitology research, 83(8), 746-754 (1997-01-01)
Identification of neo-antigenic determinant(s) on parasite infected cell surface is important to control intracellular infections. Such determinant(s) on the surface of intact Plasmodium berghei infected erythrocytes have not been conclusively demonstrated. To generate polyclonal antiserum selectively recognizing the parasite infected
Chanjae Lee et al.
Development genes and evolution, 219(6), 319-330 (2009-06-26)
One contributing factor in the worldwide decline in amphibian populations is thought to be the exposure of eggs to UV light. Enrichment of pigment in the animal hemisphere of eggs laid in the sunlight defends against UV damage, but little
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