Browse our anti-s100 (S100A1) Antibodies

Human S100 Calcium Binding Protein A1 (S100A1) interaction partners

1. The results indicate that changes in the circulating level of S100A1 protein occur in metabolic syndrome patients. The strong correlation between serum zinc-alpha2-glycoprotein and S100A1 might suggest that production or release of these two proteins could be related mechanistically.

2. The results indicated that S100A1 enhanced the ovarian cancer cell proliferation and migration.

3. found that S100B (show S100B Antibodies) plays a crucial role in blocking the interaction site between RAGE (show AGER Antibodies) V domain and S100A1. A cell proliferation assay WST (show EEF1A2 Antibodies)-1 also supported our results. This report could potentially be useful for new protein development for cancer treatment

4. Study provides evidence that mir-363 and its target S100A1 are under the regulatory function of FOXD2-AS1 aggravating nasopharyngeal carcinoma carcinogenesis.

5. X-ray crystal structure of human calcium-bound S100A1 has been reported.

6. a molecular mechanism for the potential regulation of TRPM1 (show TRPM1 Antibodies) by S100A1

7. Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 (show STIP1 Antibodies) are key players in this pathway; the stoichiometry of S100A1/STIP1 (show STIP1 Antibodies) interaction appears to be three S100A1 dimers plus one STIP1 (show STIP1 Antibodies) monomer; each S100A1-STIP1 (show STIP1 Antibodies)-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 (show STIP1 Antibodies) = stress-induced-phosphoprotein 1 (show STIP1 Antibodies)) [REVIEW]

8. Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (show STIP1 Antibodies) (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 (show STIP1 Antibodies) TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1.

9. 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.

10. a correlation between S100B (show S100B Antibodies) + A1-positive Human Articular Chondrocytes in monolayer culture and their neochondrogenesis capacity in pellet culture, is reported.

Cow (Bovine) S100 Calcium Binding Protein A1 (S100A1) interaction partners

1. identified S100A1, but not calmodulin (show KRIT1 Antibodies) or other S100 proteins, as a potent molecular chaperone (show HSP90AA1 Antibodies) and a new member of the Hsp70 (show HSP70 Antibodies)/Hsp90 (show HSP90 Antibodies) multichaperone complex (S100A1)

2. Results suggest that S100A1 can act as a linker between the calcium and redox signalling pathways.

3. beta-mercaptoethanol modification of apo (show C9orf3 Antibodies)-S100A1 makes its structure more similar to that of holo-S100A1, so that it becomes much better adjusted for calcium coordination.

Mouse (Murine) S100 Calcium Binding Protein A1 (S100A1) interaction partners

1. Data (including data from studies using knockout mice) suggest that S100A1 (S-100 calcium-binding protein (show GUCA1B Antibodies) A1 (show BCL2A1 Antibodies), alpha chain (show FCGRT Antibodies)) is involved in protein kinase A- (RIIalpha and RIIbeta (show PRKAR2B Antibodies))-dependent signaling resulting in nuclear redistribution/influx of HDAC4 (histone deacetylase 4 (show HDAC5 Antibodies)) in skeletal muscle fibers.

2. 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.

3. S100A1 and S100B (show S100B Antibodies) are dispensable for endochondral ossification during skeletal development.

4. S100A1 ablationalso reduced plaque associated and increased non-plaque associated PO4-Akt and PO4-GSK3beta staining.

5. 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 Antibodies)/MyD88 (show MYD88 Antibodies).

6. hypoxia-induced MiR (show MLXIP Antibodies)-138 is an essential mediator of EC dysfunction via its ability to target the 3'UTR (show UTS2R Antibodies) of S100A1.

7. Report downregulation of S100A1 expression in critical limb ischemia impairs postischemic angiogenesis via compromised proangiogenic endothelial cell function and nitric oxide synthase (show NOS Antibodies) regulation.

8. S100A1 and calmodulin bind to an overlapping domain on the ryanodine receptor (show RYR3 Antibodies) type 1 to tune the Ca2 (show CA2 Antibodies)+ release process, and thereby regulate skeletal muscle function. (Review)

9. The RyR1 (show RYR1 Antibodies)-L3625D mutation removed both an early activating effect of S100A1 and calmodulin and delayed the suppression of RyR1 (show RYR1 Antibodies) Ca2 (show CA2 Antibodies)+ release, providing new insights into calmodulin and S100A1 regulation of skeletal muscle excitation-contraction coupling.

10. Data suggest that the absence of S100A1 suppresses physiological AP-induced Ca(2 (show CA2 Antibodies)+) release flux, resulting in impaired contractile activation and force production in skeletal muscle.