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Mouse Anti-ANK1 Recombinant Antibody (8C3) (CBMAB-A2746-YC)

Provided herein is a Mouse monoclonal antibody against Human Ankyrin 1. The antibody can be used for immunoassay techniques, such as WB, IP, IF, IHC-P, ELISA.
See all ANK1 antibodies
Published Data
Mouse Anti-ANK1 Recombinant Antibody (8C3) in IF
Fluorescence signals in HEK293T cells which express pEGFP-C1-ANK1-WT and pEGFP-C1-ANK1-MT, showed that the ANK1 mutants failed to localize to the plasma membrane. Confocal images of ANK1 (green), DAPI nuclear staining (blue), and merged signals. ...View More
Xu, L., Wei, X., Liang, G., Zhu, D., Zhang, Y., Zhang, Y., & Shang, X. (2023). A novel splicing mutation of ANK1 is associated with phenotypic heterogeneity of hereditary spherocytosis in a Chinese family. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1869(1), 166595.
Mouse Anti-ANK1 Recombinant Antibody (8C3) in IF
Fluorescent images of co-localization results on a normal RBC, an echinocyte, and a spherocyte, respectively. Band 3 is dyed in green, ankyrin is dyed in red, and the merged color is yellow. In echinocyte and spherocyte, the linkage of Band 3 and ankyrin is dissociated. ...View More
Pan, Y., Li, Y., Li, Y., Li, J., & Chen, H. (2022). Fatigue of red blood cells under periodic squeezes in ECMO. Proceedings of the National Academy of Sciences, 119(49), e2210819119.
Mouse Anti-ANK1 Recombinant Antibody (8C3) in IP
Co-immunoprecipitation analysis on the dissociation of Band 3 and ankyrin in the fatigued RBCs (N = 15,000) compared with that in the normal RBCs (N = 0). ...View More
Pan, Y., Li, Y., Li, Y., Li, J., & Chen, H. (2022). Fatigue of red blood cells under periodic squeezes in ECMO. Proceedings of the National Academy of Sciences, 119(49), e2210819119.
Mouse Anti-ANK1 Recombinant Antibody (8C3) in Immunoblot
Immunoblot (aankyrin-1 monoclonal antibody [clone 8C3]) of fractionated RBC ghosts prepared from (1) WT (þ/þ), (2) E924X/þ, and (3) E924X/E924X blood. Arrows indicate major immunoreactive bands. ...View More
Hughes, M. R., Anderson, N., Maltby, S., Wong, J., Berberovic, Z., Birkenmeier, C. S., ... & Stanford, W. L. (2011). A novel ENU-generated truncation mutation lacking the spectrin-binding and C-terminal regulatory domains of Ank1 models severe hemolytic hereditary spherocytosis. Experimental hematology, 39(3), 305-320.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
8C3
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, IHC-P, ELISA

Basic Information

Immunogen
Ankyrin-1 from erythrocytes of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:30-1:3,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Ankyrin 1
Introduction
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane
Entrez Gene ID
Human286
Mouse11733
Rat306570
UniProt ID
HumanP16157
MouseQ02357
RatD3Z9Z0
Alternative Names
Ankyrin 1; Ankyrin 1, Erythrocytic; Erythrocyte Ankyrin; Ankyrin-R; ANK-1; ANK; Ankyrin-1; SPH1; SPH2;
Function
Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.
Isoform Mu17: Together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.
Biological Process
Cytoskeleton organization Source: UniProtKB
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: BHF-UCL
Exocytosis Source: UniProtKB
Maintenance of epithelial cell apical/basal polarity Source: UniProtKB
Positive regulation of organelle organization Source: Ensembl
Protein localization to plasma membrane Source: BHF-UCL
Signal transduction Source: InterPro
Cellular Location
Isoform Er1: Cytoskeleton. Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.
Isoform Mu17: Membrane; M line. Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells.
Isoform Mu18: Sarcoplasmic reticulum
Isoform Mu19: Sarcoplasmic reticulum
Isoform Mu20: Sarcoplasmic reticulum
Involvement in disease
Spherocytosis 1 (SPH1): A form of spherocytosis, a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH1 is characterized by severe hemolytic anemia. Inheritance can be autosomal dominant or autosomal recessive. Patients with homozygous mutations have a more severe disorder.
PTM
Regulated by phosphorylation.
Palmitoylated.
Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region. Hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region.
(Microbial infection) Probably cleaved by P.falciparum SERA6; the cleavage probably causes the disruption of the actin cytoskeleton and the rupture of the erythrocyte cell membrane releasing the merozoites.
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For research use only. Not intended for any clinical use.

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