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Purified Mouse Anti-Ankyrin B
Purified Mouse Anti-Ankyrin B

Western blot analysis of Ankyrin B. Rat brain lysates were probed with 2 µg/ml (lane 1) or 5 µg/ml (lane 2) of the mouse anti-ankyrin B antibody (clone 2.20).  Ankyrin B isoforms can be observed at ~150 and ~220 kDa, respectively.

Western blot analysis of Ankyrin B. Rat brain lysates were probed with 2 µg/ml (lane 1) or 5 µg/ml (lane 2) of the mouse anti-ankyrin B antibody (clone 2.20).  Ankyrin B isoforms can be observed at ~150 and ~220 kDa, respectively.

Product Details
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BD Pharmingen™
Rat (QC Testing), Human (Reported)
Mouse IgG1
Human Ankyrin B Spectrin Binding Domain Peptide
Western blot (Routinely Tested), ELISA, Fluorescence microscopy (Reported)
110-440 kDa
0.5 mg/ml
AB_397145
Aqueous buffered solution containing ≤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 4°C.

Recommended Assay Procedures

Western blot:  Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml. Neonatal rat brain membranes are suggested for use as the positive control.

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.
558892 Rev. 4
Antibody Details
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2.20

Ankyrins are a family of proteins which were first discovered in erythrocytes and shown to bind to spectrin, a primary component of the cytoskeletal architecture. They have since been shown to be expressed at very high levels in the vertebrate brain and are also found in other cell types. Ankyrins function by acting as adaptors to link integral membrane proteins, including cell adhesion and ion channel molecules to the cytoskeleton. The structure of ankyrin consists of three domains, two highly conserved N-terminal and one C-terminal variable domain. The conserved regions contain a membrane-binding domain of ~89-95 kDa and a spectrin-binding domain of ~62 kDa, while the variable region has pre-mRNA alternative splice sites. Two ankyrins have been extensively characterized: ankryin R is the product of the ANK1 gene and is primarily expressed in the brain, although alternatively spliced forms are found in erythrocytes; ankyrin B is the product of the ANK2 gene, located on a different chromosome from ANK1, and is primarly expressed in neonatal and adult brain but is also found in heart, lymphocytes and platelets. Studies done on ankyrinB (-/-) knockout mice, which die by postnatal day 21, have demonstrated a link between the L1 cell adhesion molecule and ankyrin B in premyelinated axons. Isoforms of ankyrin B have been reported to be detectable ranging from approximately 440, 220, 150 and 110 kDa in western blot analysis, depending on the tissue-type of origin.

This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.

558892 Rev. 4
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
558892 Rev.4
Citations & References
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Development References (5)

  1. Bennett V, Gilligan DM. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol. 1993; 9:27-66. (Biology). View Reference
  2. Kordeli E, Davis J, Trapp B, Bennett V. An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J Cell Biol. 1990; 110(4):1341-1352. (Biology: ELISA, Fluorescence microscopy, Western blot). View Reference
  3. Kordeli E, Lambert S, Bennett V. AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J Biol Chem. 1995; 270(5):2352-2359. (Biology). View Reference
  4. Otto E, Kunimoto M, McLaughlin T, Bennett V. Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J Cell Biol. 1991; 114(2):241-253. (Biology: ELISA, Fluorescence microscopy, Western blot). View Reference
  5. Scotland P, Zhou D, Benveniste H, Bennett V. Nervous system defects of AnkyrinB (-/-) mice suggest functional overlap between the cell adhesion molecule L1 and 440-kD AnkyrinB in premyelinated axons. J Biol Chem. 1998; 143(5):1305-1315. (Biology). View Reference
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558892 Rev. 4

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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.