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Cow (Bovine) Actin ELISA Kit for Sandwich ELISA - ABIN1874334
Bobowiec, Wojcik, Jaworska-Adamu, Tusinska: Fibrogenic response of hepatic stellate cells in ovariectomised rats exposed to ketogenic diet. in Journal of physiology and pharmacology : an official journal of the Polish Physiological Society 2013
Shorter than normal thin filament length contributes to the impaired force generation in patients with thin filament myopathy, but only in those who harbor specific mutations in NEB (show NEB ELISA Kits) or ACTA1.
Over-expression of TNC (show TNC ELISA Kits), SMA (show SMN1 ELISA Kits), and vimentin (show VIM ELISA Kits) were significantly correlated with the lower overall survival in prostate cancer patients.
ANA (show BTG3 ELISA Kits) and ASMA evaluation in patients with liver transplantation and no history of autoimmune disease has no clinical relevance, since it varies in time and is not related to any risk factors or liver injury. Routine autoimmunity evaluation should be avoided.
Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the vinculin tail helical bundle to mediate actin bundling.
This study reported the new information on the frequency and phenotypes of congenital myopathy caused by ACTA1 mutations in subjects >/=5 years of age.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Mutations in ACTA1 can cause pathologic features consistent with myofibrillar myopathy.
TIMP-1 (show TIMP1 ELISA Kits) significantly increased levels of alpha-SMA (show SMN1 ELISA Kits).
Myopathy associated with zebra bodies is part of the spectrum of myopathies associated with the ACTA1 gene.
New scapuloperoneal phenotype associated with an ACTA1 mutation.
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
alpha smooth muscle actin (show ACTG2 ELISA Kits) (alphaSMA (show ACTA2 ELISA Kits)) was identified as a marker of osteoprogenitor cells in bone and periodontium.
WIP is a link between membrane lipid composition and actin cytoskeleton at dendritic spines.
ACTA1(Asp286Gly) mouse model of nemaline myopathy provide evidence of impaired in vivo muscle function, altered muscle structure and disturbed energy metabolism.
Combined MRI (show C7ORF49 ELISA Kits) and (3)(1)P-MRS investigations of the ACTA1(H40Y) mouse model of nemaline myopathy show impaired muscle function and altered energy metabolism.
Data indicate roles for linkers of nucleus to cytoskeleton (LINC) molecules nesprin2giant and nesprin3, which anchor actin cap fibers to the nucleus.
Asp286Gly acts as a "poison-protein" and according to the computational analysis it modifies the actin-actin interface. This phenomenon is likely to prevent proper myosin cross-bridge binding.
Data show that upon actin binding, the two domains of utrophin (show UTRN ELISA Kits) become dramatically separated and ordered, indicating a transition to a single open and extended conformation.
Data indicated that CacyBP/SIP (show CACYBP ELISA Kits) could simultaneously interact with tubulin (show TUBB ELISA Kits) and actin, suggesting that CacyBP/SIP (show CACYBP ELISA Kits) might link actin and tubulin (show TUBB ELISA Kits) cytoskeletons.
Results provide the genetic proof that platelet production from megakaryocytes strictly requires dynamic changes in the actin cytoskeleton.
Data show that while increases in cardiac and vascular smooth-muscle actin can partially compensate for the lack of skeletal actin in null mice, this is not sufficient to support adequate skeletal muscle growth and/or function.
The product encoded by this gene belongs to the actin family of proteins, which are highly conserved proteins that play a role in cell motility, structure and integrity. Alpha, beta and gamma actin isoforms have been identified, with alpha actins being a major constituent of the contractile apparatus, while beta and gamma actins are involved in the regulation of cell motility. This actin is an alpha actin that is found in skeletal muscle. Mutations in this gene cause nemaline myopathy type 3, congenital myopathy with excess of thin myofilaments, congenital myopathy with cores, and congenital myopathy with fiber-type disproportion, diseases that lead to muscle fiber defects.
actin, alpha 1, skeletal muscle
, actin, alpha skeletal muscle
, nemaline myopathy type 3
, alpha actin 1
, skeletal alpha actin
, actin alpha 1