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Purified Mouse Anti-β-Spectrin II
Purified Mouse Anti-β-Spectrin II

Western blot analysis of β-Spectrin II on Jurkat lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of β-Spectrin II.

Purified Mouse Anti-β-Spectrin II

Immunofluorescent staining of Hela cells grown on microscope slides with β-Spectrin II  monoclonal antibody.

Western blot analysis of β-Spectrin II on Jurkat lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of β-Spectrin II.

Immunofluorescent staining of Hela cells grown on microscope slides with β-Spectrin II  monoclonal antibody.

Product Details
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BD Transduction Laboratories™
Human (QC Testing), Mouse, Rat, Dog (Tested in Development)
Mouse IgG1
Human β-Spectrin II aa. 2101-2189
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
280 kDa
250 µg/ml
AB_399853
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

For western blot analysis use at 1:1000. Detailed protocol is available at: http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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Antibody Details
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42/B-Spectrin II

Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and ß, which intertwine to form heterodimers that can self associate into elongated tetramers. α-spectin I and ß-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectin I and II with ß-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats alongwith various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. α-spectrin II is a widely expressed non-erythroid α-spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites for proteases, such as calpains and caspase-3. ß-spectrin II is a widely expressed non-erythroid ß-spectrin that contains a C-terminal region that interacts with α-spectrins and a PH domain. α-spectrin II and ß-spectrin II, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with Band 4.1, F-actin, and other proteins near the plasma membrane. This scaffold of cytoskeletal and plasma membrane proteins is critical for the maintenance of cell structure.

This antibody is routinely tested by the Western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only.

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Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
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Citations & References
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Development References (3)

  1. Hu RJ, Watanabe M, Bennett V. Characterization of human brain cDNA encoding the general isoform of beta-spectrin. J Biol Chem. 1992; 267(26):18715-18722. (Biology). View Reference
  2. Moon RT, McMahon AP. Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin. J Biol Chem. 1990; 265(8):4427-4433. (Biology). View Reference
  3. Nicolas G, Fournier CM, Galand C, et al. Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. Mol Cell Biol. 2002; 22(10):3527-3536. (Biology). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.