Anti-Ankyrin-G (Staining) Antibody (N106/65)

15 Citations

Our Anti-Ankyrin-G (Staining) mouse monoclonal primary antibody from NeuroMab is produced in-house from hybridoma clone N106/65. It detects human, mouse, and rat Ankyrin-G (Staining), and is purified by Protein A chromatography. It is great for use in IHC, ICC.

Immunofluorescence labeling of axon initial segments in adult rat cortex with N106/65 TC supe (red) and Hoechst nuclear stain (blue).
Immunofluorescence labeling of axon initial segments in adult rat cortex with N106/65 TC supe (red) and Hoechst nuclear stain (blue).
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Immunofluorescence labeling of axon initial segments in adult rat cortex with N106/65 TC supe (red) and Hoechst nuclear stain (blue).
Representative images showed the high expression level of FKBP12 (green) in axonal hillock/axon initial segment (labeled by anti–ankyrin-G antibody, cat. 75-147; bright blue) under basal conditions whereas FKBP12 translocated to soma and dendrites when neurons bear tau aggregation. Image from publication CC-BY-4.0. PMID:36724228

Human, Mouse, Rat
EM, ICC, IHC
Mouse
490
550
594
650
Carrier-Free

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Data Sheet
Trial Size Trial Size

SKU: 75-147

Volume: 100 µL
Price:
$385.00
Ships: 1-2 business days

Product Details

Ankyrin-G (Staining)
Ankyrin-G (ankyrin 3) is a member of the Ankyrin family which consists of Ankyrin R (1), Ankyrin B (2) and Ankyrin G (3) all of which are expressed in the nervous system. Ankyrins are structural proteins that aid in the attachment of integral membrane proteins with the spectrin-actin cytoskeleton, and thus targets voltage-gated sodium channels, potassium channels, cell adhesion molecules and others at the nodes of Ranvier and axonal initial segments (AIS). Variants in Ankyrin G have been linked to bipolar disorder.
Purified by Protein A chromatography
1 mg/mL
Monoclonal
N106/65
IgG2b
EM, ICC, IHC
Mouse
ANK3
<200 kDa
Fusion protein ~1000 amino acids of Ankyrin-G (accession number E9PE32) produced recombinantly in E. Coli
Human, Mouse, Rat
AB_10675130
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.74
IHC: 1:500
ICC: 1:500
Unconjugated
Does not cross-react with Ankyrin-B
Each new lot of antibody is quality control tested by IHC on either rat or mouse brain and confirmed to give the expected staining pattern.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
24 months from date of receipt
Shipped on ice packs
Ankyrin-3 (ANK-3) (Ankyrin-G)
E9PE32

Product Specific References for Applications and Species

Immunocytochemistry: Mouse
PMID Dilution Publication
39626668not listedFalahati, H., et al. 2024. Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation. Current Biology, .
327328891:100Yang, C., et al. 2020. Targeting QKI-7 in vivo restores endothelial cell function in diabetes. Nature Communications, 3812.
Immunocytochemistry: Rat
PMID Dilution Publication
382520801:200Rentsch, J, et al. 2024. Sub-membrane actin rings compartmentalize the plasma membrane. The Journal of Cell Biology, .
Immunohistochemistry: Human
PMID Dilution Publication
2702940510ug/mlde Bruin, R.G., et al. 2014. Quaking promotes monocyte differentiation into pro-atherogenic macrophages by controlling pre-mRNA splicing and gene expression.. Nature Communications, 10846.
23963726not listedvan der Veer, E.P., et al. 2013. Quaking, an RNA-binding protein, is a critical regulator of vascular smooth muscle cell phenotype.. Circulation Research, 1065-1075.
Immunohistochemistry: Mouse
PMID Dilution Publication
392513521:200Melton, A.J., et al. 2024. TRIM46 is required for microtubule fasciculation in vivo but not axon specification or axon initial segment formation. The Journal of Neuroscience, .
38985877not listedFrüh, S., et al. 2024. Monoallelic de novo AJAP1 loss-of-function variants disrupt trans-synaptic control of neurotransmitter release. Science Advances, eadk5462.
368306391:500De Nuccio, F., et al. 2023. Oligodendrocytes Prune Axons Containing α-Synuclein Aggregates In Vivo: Lewy Neurites as Precursors of Glial Cytoplasmic Inclusions in Multiple System Atrophy?. Biomolecules, 269.
274543261:100Bin, J.M., et al. 2016. The oligodendrocyte-specific antibody ''CC1'' binds Quaking 7.. Journal of Neurochemistry, 181-186.
27196066not listedSuiko, T., et al. 2016. Expression of Quaking RNA-Binding Protein in the Adult and Developing Mouse Retina. PLoS One, e0156033.
Western Blot: Human
PMID Dilution Publication
35544276not listedFagg, W.S., et al. 2022. Definition of germ layer cell lineage alternative splicing programs reveals a critical role for Quaking in specifying cardiac cell fate. Nucleic acids research, 5313-5334.
244499171:1000Chan, C.B., et al. 2014. PIKE is essential for oligodendroglia development and CNS myelination.. PNAS: USA, 1993-1998.
Western Blot: Mouse
PMID Dilution Publication
327328891:1000Yang, C., et al. 2020. Targeting QKI-7 in vivo restores endothelial cell function in diabetes. Nature Communications, 3812.
274543261:1000Bin, J.M., et al. 2016. The oligodendrocyte-specific antibody ''CC1'' binds Quaking 7.. Journal of Neurochemistry, 181-186.
27196066not listedSuiko, T., et al. 2016. Expression of Quaking RNA-Binding Protein in the Adult and Developing Mouse Retina. PLoS One, e0156033.

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