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Key Documents

S1515

Sigma-Aldrich

Anti-Spectrin antibody produced in rabbit

whole antiserum

Synonyme(s) :

Anti-EL2, Anti-HPP, Anti-HS3, Anti-SPH3, Anti-SPTA

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

whole antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Contient

15 mM sodium azide

Espèces réactives

human

Technique(s)

western blot: 1:400

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

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.

Spécificité

The antibody reacts specifically with the α and β chains of human erythrocyte spectrin.

Immunogène

spectrin from freshly prepared human erythrocyte ghosts.

Application

Anti-Spectrin antibody has been used in western blotting immunofluorescence and immunostaining.

Actions biochimiques/physiologiques

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.

Clause de non-responsabilité

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.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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
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
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)
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.
F Galbiati et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(17), 9689-9694 (2000-08-10)
It recently was reported that Duchenne muscular dystrophy (DMD) patients and mdx mice have elevated levels of caveolin-3 expression in their skeletal muscle. However, it remains unknown whether increased caveolin-3 levels in DMD patients contribute to the pathogenesis of DMD.

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