Anti-S100A1: Mouse S100A1 Antibody

S100A1, a Ca²⁺ binding protein of the EF-hand type, is preferentially expressed in myocardial tissue and has been found to colocalize with the sarcoplasmic reticulum (SR) and the contractile filaments in cardiac tissue. S100A1 is known to modulate SR Ca²⁺ handling in skeletal muscle. Moreover, recent studies revealed a differential expression of S100A1 with diminished protein levels in cardiomyopathy, whereas in compensated hypertrophy S100A1 protein was found to be up-regulated. Thus, alterations in the expression of this protein might very well contribute to impaired sarcoplasmic Ca²⁺ handling in end-stage heart failure.² It is suggested that S100A1 might be involved in the regulation of cardiac contractility. S100A1 improves cardiac contractile performance both by regulating SR Ca²⁺ handling and myofibrillar Ca²⁺ responsiveness.³ In addition it has been shown that the S100A1 protein is released into the extracellular space in considerable amounts during ischemic myocardial injury via an unknown mechanism. he extracellular S100A1 protein can protect cardiomyocytes from apoptosis based on Ca²⁺-dependent clathrin-mediated endocytotic uptake resulting in a specific activation of the pro-survival ERK1/2 signaling pathway.⁴ Moreover, S100A1 acts as a potent molecular chaperone and a new cochaperone protein of the Hsp70/Hsp90 multichaperone complex.