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Rat (Rattus) s100 ELISA Kit for Sandwich ELISA - ABIN416487
Yang, Song, Zhao, Qiu, Hu, Chang: Vasoactive intestinal peptide protects against ischemic brain damage induced by focal cerebral ischemia in rats. in Brain research 2011
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Rat (Rattus) s100 ELISA Kit for Sandwich ELISA - ABIN850655
Yu, Lu, Li, Xiao, Xing, Li, Wu: Role of S100A1 in hypoxia-induced inflammatory response in cardiomyocytes via TLR4/ROS/NF-?B pathway. in The Journal of pharmacy and pharmacology 2015
Cow (Bovine) s100 ELISA Kit for Sandwich ELISA - ABIN414047
Sun, Cao, Cai, Li, Yu, Yao: Regulation of Nutritional Metabolism in Transition Dairy Cows: Energy Homeostasis and Health in Response to Post-Ruminal Choline and Methionine. in PLoS ONE 2016
identified S100A1, but not calmodulin (show KRIT1 ELISA Kits) or other S100 proteins, as a potent molecular chaperone (show HSP90AA1 ELISA Kits) and a new member of the Hsp70 (show HSP70 ELISA Kits)/Hsp90 (show HSP90 ELISA Kits) multichaperone complex (S100A1)
Results suggest that S100A1 can act as a linker between the calcium and redox signalling pathways.
beta-mercaptoethanol modification of apo (show C9orf3 ELISA Kits)-S100A1 makes its structure more similar to that of holo-S100A1, so that it becomes much better adjusted for calcium coordination.
Levels of NSE (show ENO2 ELISA Kits) and S100B (show S100B ELISA Kits) are still elevated 1 year postpartum in women who have had preeclampsia in contrast to women with previous normal pregnancies.
In vitro experiments using repeated freeze-thaw procedures showed an intracellular up-regulation of S100B (show S100B ELISA Kits) in normal and vitiligo (show MITF ELISA Kits) melanocytes before an extensive release in the environment.
Acute paranoid schizophrenia inpatients present a day/night change of S100B (show S100B ELISA Kits) serum levels at admission that disappears at discharge.
Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 (show STIP1 ELISA Kits) are key players in this pathway; the stoichiometry of S100A1/STIP1 (show STIP1 ELISA Kits) interaction appears to be three S100A1 dimers plus one STIP1 (show STIP1 ELISA Kits) monomer; each S100A1-STIP1 (show STIP1 ELISA Kits)-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 (show STIP1 ELISA Kits) = stress-induced-phosphoprotein 1 (show STIP1 ELISA Kits)) [REVIEW]
Compared to the control, the S100B (show S100B ELISA Kits)/GAPDH (show GAPDH ELISA Kits) mRNA ratio was significantly decreased in chronic liver diseases (p = 0.006) and most decreased in chronic hepatitis C patients (p = 0.023). We here evaluated S100B (show S100B ELISA Kits) expression as a marker of hepatic nerves in patients with various chronic liver diseases, topographically and semi-quantitatively.
results indicate there were decreased S100B (show S100B ELISA Kits) serum levels in bipolar patients in a manic phase after treatment.
Studies indicate that S100 calcium binding protein B protein (S100B (show S100B ELISA Kits)) has high affinity for zinc (Zn2+).
Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (show STIP1 ELISA Kits) (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 (show STIP1 ELISA Kits) TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1.
Results identified amino acids motif in S100A1 for protein binding to 2-oxohistidine which appears to be an evolutionarily conserved capacity from bacteria to human.
For patients recruited = 6 h after trauma, the CT-positive group indicated significantly higher levels of both H-FABP (show FABP3 ELISA Kits) and S100B (show S100B ELISA Kits) than the CT-negative group.
Data (including data from studies using knockout mice) suggest that S100A1 (S-100 calcium-binding protein (show GUCA1B ELISA Kits) A1 (show BCL2A1 ELISA Kits), alpha chain (show FCGRT ELISA Kits)) is involved in protein kinase A- (RIIalpha and RIIbeta (show PRKAR2B ELISA Kits))-dependent signaling resulting in nuclear redistribution/influx of HDAC4 (histone deacetylase 4 (show HDAC5 ELISA Kits)) in skeletal muscle fibers.
S100A1-KO exhibited increased right ventricular (RV) weight and elevated RV pressure in the absence of altered left ventricular filling pressures, increase in wall thickness of muscularized pulmonary arteries and a reduction in microvascular perfusion.
S100A1 and S100B (show S100B ELISA Kits) are dispensable for endochondral ossification during skeletal development.
S100A1 ablationalso reduced plaque associated and increased non-plaque associated PO4-Akt (show AKT1 ELISA Kits) and PO4-GSK3beta (show GSK3b ELISA Kits) staining.
Patients with acute myocardial infarction (MI) showed significantly increased S100A1 serum levels. Experimental MI in mice induced comparable S100A1 release. S100A1 signaling in cardiac fibroblasts occurs through endosomal TLR4 (show TLR4 ELISA Kits)/MyD88 (show MYD88 ELISA Kits).
hypoxia-induced MiR (show MLXIP ELISA Kits)-138 is an essential mediator of EC dysfunction via its ability to target the 3'UTR (show UTS2R ELISA Kits) of S100A1.
Report downregulation of S100A1 expression in critical limb ischemia impairs postischemic angiogenesis via compromised proangiogenic endothelial cell function and nitric oxide synthase (show NOS ELISA Kits) regulation.
S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor (show RYR3 ELISA Kits) type 1 to tune the Ca2 (show CA2 ELISA Kits)+ release process, and thereby regulate skeletal muscle function. (Review)
The RyR1 (show RYR1 ELISA Kits)-L3625D mutation removed both an early activating effect of S100A1 and calmodulin and delayed the suppression of RyR1 (show RYR1 ELISA Kits) Ca2 (show CA2 ELISA Kits)+ release, providing new insights into calmodulin and S100A1 regulation of skeletal muscle excitation-contraction coupling.
Data suggest that the absence of S100A1 suppresses physiological AP-induced Ca(2 (show CA2 ELISA Kits)+) release flux, resulting in impaired contractile activation and force production in skeletal muscle.
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21\; however, this gene is located at 21q22.3. This protein may function in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.
S100 calcium binding protein A1
, S100 calcium binding protein A1-like
, Protein S100-A1
, S-100 protein alpha chain
, S-100 protein subunit alpha
, S100 alpha
, S100 calcium-binding protein A1
, S100 protein, alpha polypeptide
, protein S100-A1
, protein S100-A13
, S-100 calcium-binding protein, beta chain
, S-100 protein subunit beta
, S100 calcium-binding protein, beta (neural)
, protein S100-B