Anti-Alpha-Spectrin, N-terminal 80 kDa Domain Antibody

This rabbit IgG polyclonal antibody was generated against human red blood cell a-spectrin N terminal 1/4th and is specific for human red blood cell a-spectrin N terminal 1/4th of the protein.

Highlights:

  • Reacts with human red blood cell a-spectrin N terminal 1/4th of the protein
  • Recommended for Western Blot applications

Spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane in eukaryotic cells along with actin. Spectrin plays a role in cell shape control, arrangement of transmembrane proteins, and organelle positioning. Specifically, Alpha-spectrin is a tetramer and mutations in alpha-spectrin can result in a variety of hereditary red blood cell disorders (e.g. spherocytic hemolytic anemia including elliptocytosis type 2, pyropoikilocytosis).

From the laboratories of David W. Speicher, PhD, The Wistar Institute.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EWI029
Anti-Alpha-Spectrin, N-terminal 80 kDa Domain Antibody
50uL In stock
Regular Price:$306.00
On Sale:
Specifications

Product Type: Antibody
Alternative Name(s): Erythroid alpha-spectrin,Spectrin alpha chain, erythrocytic 1
Antigen: Human Red Blood Cell a-Spectrin N terminal 1/4th of the protein
Accession ID: HGNC: 11272 Ensembl: ENSG00000163554 OMIM: 182860 Entrez Gene: 6708 UniProtKB: P02549
Molecular Weight: 280 kDa
Isotype: IgG
Clonality: Polyclonal
Reactivity: Human
Immunogen: Alpha-spectrin 80kDa domain (approximately residues 7-601)
Species Immunized: Rabbit
Tested Applications: Western Blot (1: 500,000; 5sec exposure)
Storage: -80C
Shipped: Dry ice

Data

Western Blot

Lane 1, Human Red Cell Membrane; Lane 2, Human Melanoma (1205 LU); Lane 3, Human Ovarian Cancer (RMG1); Lane 4, Human Ovarian Cancer (OV90). Gel loads: Lane 1, 5mg; Lanes 2-4, 25mg. Antibody dilution: 1:500,000, 5sec exposure.

Provider
From the laboratories of David W. Speicher, PhD, The Wistar Institute.
References
  1. Speicher DW, DeSilva TM, Speicher KD, Ursitti JA, Hembach P, Weglarz L. Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J Biol Chem. 1993 Feb 25;268(6):4227-35.
  2. Zimmerman UJ, Speicher DW, Fisher AB. Secretagogue-induced proteolysis of lungspectrin in alveolar epithelial type II cells. Biochim Biophys Acta. 1992 Oct27;1137(2):127-34.
  3. Speicher DW, DeSilva TM, Speicher KD, Ursitti JA, Hembach P, Weglarz L.Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J Biol Chem. 1993 Feb 25;268(6):4227-35.
  4. Kotula L, DeSilva TM, Speicher DW, Curtis PJ.Functional characterization of recombinant human red cell alpha-spectrin polypeptides containing the tetramer binding site.J Biol Chem. 1993 Jul 15;268(20):14788-93.

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