Anti-Ankyrin-G Antibody, clone N106/36

Recombinant protein corresponding to human Ankyrin-G.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2a κ in 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Control
Rat hippocampus tissue

Evaluated by Immunohistochemistry in rat hippocampus tissue.

Immunohistochemistry Analysis: A 1:500 dilution from a representative lot detected Ankyrin-G in rat hippocampus tissue.

Anti-Ankyrin-G Antibody, clone N106/36 is a highly specific mouse monoclonal antibody & that targets Ankyrin & has been tested in IHC.

Immunohistochemistry Analysis: A 1:2,000 dilution from a representative lot detected Ankyrin-G in rat cerebral cortex tissue.

Immunohistochemistry Analysis: A representative lot detected Ankyrin-G in rat optic nerve tissue.

Immunofluorescence Analysis: A representative lot detected Ankyrin-G in adult rat cortex tissue.

Immunofluorescence Analysis: A representative lot from an independent laboratory detected Ankyrin-G in a rat model of TLE mEC layer II neurons (Hargus, N. J., et al. (2011). Neurobiol Dis. 41(2):361-376.)

Research Category
Neuroscience

Research Sub Category
Developmental Neuroscience

Other homologies: Human (92% sequence homology), and Mouse (87% sequence homology).

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.

480 kDa calculated

Ankyrins are a family of spectrin-binding proteins that couple the spectrin/actin cytoskeletal network to the cytoplasmic domains of integral membrane proteins which include channels such as the anion exchanger, voltage-dependent sodium channel, and the Na/K ATPase, as well as neuronal cell adhesion molecules related to L1. In the nervous system, three different ankyrins are known to exist; ankyrinB, ankyrinG, and ankyrinR. All three ankyrins contain an N-terminal membrane binding domain, an internal domain capable of binding spectrin, and a C-terminal regulatory domain which is the target of alternative splicing. AnkyrinB, the predominant neuronal ankyrin includes two isoforms of ~220 kDa and ~440 kDa. The ~220 kDa alternatively spliced isoform is the major form present in the adult brain, while the ~440 kDa form is preferentially expressed in the developing neonatal brain. Three forms of ankyrinG (~190 kDa, ~270 kDa, ~480 kDa) are localized in axonal initial segments and the nodes of Ranvier of myelinated axons where fluxes of action potential occur and ion channels are enriched. Ankyrins comprise ~0.5%-1% of the total membrane protein in the adult vertebrate brain.

Stable for 1 year at 2-8°C from date of receipt.