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Data suggest that kindlin-2 (Kind2/Fermt2 (zeige FERMT2 Proteine)) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1 (zeige ITGB1 Proteine)) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 (zeige FERMT2 Proteine) leads to dissociation of Actn2 and Itgb1 (zeige ITGB1 Proteine).
Data show that alpha-Actinin 2 and CaMKIIalph (zeige NEXN Proteine)a exist in complex with GluN2B in forebrain.
Data demonstrated that the Z-disk proteins, ZASP (zeige LDB3 Proteine), titin (zeige TTN Proteine) and vinculin (zeige VCL Proteine) preferentially bind to alpha-actinin-2. Thus, the loss of alpha-actinin-3 (zeige ACTN3 Proteine) changes the overall protein composition of fast fiber Z-disks and alters their elastic properties.
alpha-Actinin (zeige ACTN1 Proteine), rapsyn (zeige RAPSN Proteine), and surface AChR form a ternary complex.
BPAG1 (zeige DST Proteine)-b was detectable in vitro and in vivo as a high molecular mass protein in striated (zeige NSDHL Proteine) 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 (zeige DES Proteine).
demonstrate that proper membrane localization of a small-conductance Ca(2 (zeige CA2 Proteine)+)-activated K(+) channel (zeige KCNC4 Proteine) (SK2 (zeige PAPSS2 Proteine) or K(Ca)2.2) is dependent on its interacting protein, alpha-actinin2, a major F-actin crosslinking protein (zeige MACF1 Proteine).
These results provide new insights into the regulation of SK2 channel trafficking by the cytoskeletal proteins FLNA (zeige FLNA Proteine) and alpha-actinin2, involving distinct recycling pathways
the interaction between GNE (zeige GNE Proteine) and alpha-actinin 1 (zeige ACTN1 Proteine) and alpha-actinin 2 occur at different sites in the alpha-actinin (zeige ACTN1 Proteine) molecules and that for alpha-actinin 2 the interaction site is located at the C-terminus of the protein.
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 (zeige NSDHL Proteine) muscle and explore its functional implications on the biochemical and cellular level.
This study generated the genomic sequences of K88-positive and F18 (zeige MAMLD1 Proteine)-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 (zeige CAMK2G Proteine) regulatory domain.
data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 (zeige ACTN3 Proteine) evolved differences to optimize their functions
This is the first genome-wide linkage analysis that shows mutations in ACTN2 cause HCM
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