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Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Additionally we are shipping ACTN2 Antibodies (85) and ACTN2 Kits (21) and many more products for this protein.
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Data suggest that kindlin-2 (Kind2/Fermt2 (show FERMT2 Proteins)) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1 (show ITGB1 Proteins)) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 (show FERMT2 Proteins) leads to dissociation of Actn2 and Itgb1 (show ITGB1 Proteins).
Data show that alpha-Actinin 2 and CaMKIIalph (show NEXN Proteins)a exist in complex with GluN2B in forebrain.
Data demonstrated that the Z-disk proteins, ZASP (show LDB3 Proteins), titin (show TTN Proteins) and vinculin (show VCL Proteins) preferentially bind to alpha-actinin-2. Thus, the loss of alpha-actinin-3 (show ACTN3 Proteins) changes the overall protein composition of fast fiber Z-disks and alters their elastic properties.
alpha-Actinin (show ACTN1 Proteins), rapsyn (show RAPSN Proteins), and surface AChR form a ternary complex.
BPAG1 (show DST Proteins)-b was detectable in vitro and in vivo as a high molecular mass protein in striated (show NSDHL Proteins) 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 (show DES Proteins).
demonstrate that proper membrane localization of a small-conductance Ca(2 (show CA2 Proteins)+)-activated K(+) channel (show KCNC4 Proteins) (SK2 (show PAPSS2 Proteins) or K(Ca)2.2) is dependent on its interacting protein, alpha-actinin2, a major F-actin crosslinking protein (show MACF1 Proteins).
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 (show NSDHL Proteins) muscle and explore its functional implications on the biochemical and cellular level.
This study generated the genomic sequences of K88-positive and F18 (show MAMLD1 Proteins)-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 (show CAMK2G Proteins) regulatory domain.
data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 (show ACTN3 Proteins) 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 (show DMD Proteins) and alpha-actinin-2 are not functionally interchangeable.
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