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anti-Mouse (Murine) ACTN2 Antibodies:
anti-Rat (Rattus) ACTN2 Antibodies:
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Human Monoclonal ACTN2 Primary Antibody for IHC (fro), IHC (p) - ABIN3043675
Xiao, Zhang, Wang, Xu, Yu, Shen: Activation of an apoptotic signal transduction pathway involved in the upregulation of calpain and apoptosis-inducing factor in aldosterone-induced primary cultured cardiomyocytes. in Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association 2013
Show all 6 Pubmed References
Cow (Bovine) Polyclonal ACTN2 Primary Antibody for IHC, WB - ABIN2776829
Bos, Theis, Tajik, Gersh, Ommen, Ackerman: Relationship between sex, shape, and substrate in hypertrophic cardiomyopathy. in American heart journal 2008
Show all 2 Pubmed References
Human Polyclonal ACTN2 Primary Antibody for ICC, IF - ABIN442430
Meyers, Heitzman, Krebsbach, Aufdembrink, Hughes, Bartolomucci, Townsend: Acute AT1R blockade prevents isoproterenol-induced injury in mdx hearts. in Journal of molecular and cellular cardiology 2019
Data suggest that kindlin-2 (Kind2/Fermt2) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to dissociation of Actn2 and Itgb1.
Data show that alpha-Actinin 2 and CaMKIIalpha exist in complex with GluN2B in forebrain.
Data demonstrated that the Z-disk proteins, ZASP, titin and vinculin preferentially bind to alpha-actinin-2. Thus, the loss of alpha-actinin-3 changes the overall protein composition of fast fiber Z-disks and alters their elastic properties.
alpha-Actinin, rapsyn, and surface AChR form a ternary complex.
BPAG1-b was detectable in vitro and in vivo as a high molecular mass protein in striated and heart muscle cells, co-localizing with alpha-actinin-2 and partially with the cytolinker plectin as well as with the intermediate filament protein desmin.
demonstrate that proper membrane localization of a small-conductance Ca(2+)-activated K(+) channel (SK2 or K(Ca)2.2) is dependent on its interacting protein, alpha-actinin2, a major F-actin crosslinking protein.
A novel, likely pathogenic mutation (c.959T>G/p.L320R) of ACTN2 was identified in all individuals affected with dilated cardiomyopathy (DCM) and/or ventricular tachycardia. This study not only expands the spectrum of ACTN2 mutations and contributes to the genetic diagnosis and counseling of families with DCM and arrhythmia, but also provides a new case with overlap phenotype caused by an ACTN2 variant.
A dual-beam optical tweezers measured the mechanics of alpha-actinin 2 and rabbit titin interaction at the single-molecule level. Depending on the direction of force application, the unbinding forces can more than triple. Multiple alpha-actinin/Z-repeat interactions cooperate to ensure long-term stable titin anchoring, while allowing the individual components to exchange dynamically.
These results provide new insights into the regulation of SK2 channel trafficking by the cytoskeletal proteins FLNA and alpha-actinin2, involving distinct recycling pathways
the interaction between GNE and alpha-actinin 1 and alpha-actinin 2 occur at different sites in the alpha-actinin molecules and that for alpha-actinin 2 the interaction site is located at the C-terminus of the protein.
The full length mEos2 tagged protein expressed in adult cardiomyocytes shows that both mutations additionally affect Z-disc localization and dynamic behaviour
study strengthens the hypothesis that ACTN2 influences caries risk.
The novel heterozygous missense sequence variant ACTN2 cosegregated with a complex cardiomyopathic trait, characterized by the interplay of midapical, nonobstructive HCM, early onset of AF and AV block, as well as regional LV noncompaction.
Clinical evaluation of an Australian family revealed diverse cardiac pathologies in four affected members and genetic testing of the exome identified a pathogenic ACTN2 heterozygous variant (Ala119Thr) that co-segregated with disease.
Study reports a complete high-resolution structure of the 200 kDa alpha-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level.
This study generated the genomic sequences of K88-positive and F18-positive porcine enteroteoxigenic E. coli (ETEC) strains and examined the phylogenetic distribution of clinical porcine ETEC strains and their plasmid-associated genetic content.
Findigs show that the F-actin-binding protein alpha-actinin-2 targets CaMKIIalpha to F-actin in cells by binding to the CaMKII regulatory domain.
data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 evolved differences to optimize their functions
This is the first genome-wide linkage analysis that shows mutations in ACTN2 cause HCM
Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable.
Association of Ca2+-activated K+ channel with alpha-actinin2 localizes channel to entry of external Ca(2+) source, which regulates channel function.
actinin-2 participate in sequestering parafibromin in the cytoplasmic compartment.
ACTN2 expression is affected by the content of alpha-actinin-3.
alpha-Actinin2 is required for the lateral alignment of Z discs and ventricular chamber enlargement during zebrafish cardiogenesis.
Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a muscle-specific, alpha actinin isoform that is expressed in both skeletal and cardiac muscles.
actinin, alpha 2
, alpha 2 actinin
, F-actin cross-linking protein
, alpha-actinin skeletal muscle