Anti-BAAT (aa 1-254) polyclonal antibody

Energy storage devices (ESD), such as UPS batteries, have been repurposed in datacenter as a promising tuning knob for peak power shaving and power cost reducing. However, batteries progressively aging due to irregular usage patterns, which result in less effective capacity and even pose serious threat to server availability. Nevertheless, prior proposals largely ignore the aging issues of battery which may lead to low energy availability for datacenter servers. To fill this critical void, we thoroughly investigate battery aging on a heavily instrumented prototype system over an observation period of ten months. We propose Battery Anti-Aging Treatment Plus (BAAT-P), a novel power delivery architecture included aging management algorithms from the perspective of computing system to hide, reduce, mitigate and plan the battery aging effects for high energy availability in datacenter. Our techniques exploit diverse battery aging mechanisms and dynamic aging management algorithms to provide system-level availability guarantee for datacenter. We evaluate the BAAT-P design with a real prototype. Compared with a battery powered datacenter without aging management policies, the results show that BAAT-P can extend battery lifetime by 72 percent, reduce battery cost by 33 percent and effectively improve energy availability for datacenter servers while maintaining workload performance for the performance critical workloads.

Caveolae are a subtype of cholesterol-enriched lipid microdomains/rafts that are routinely detected as vesicles pinching off from the plasma membrane. Caveolin-1 is an essential component of caveolae. Hepatic caveolin-1 plays an important role in liver regeneration and lipid metabolism. Expression of caveolin-1 in hepatocytes is relatively low, and it has been suggested to also reside at other subcellular locations than the plasma membrane. Recently, we found that the peroxisomal membrane contains lipid microdomains. Like caveolin-1, hepatic peroxisomes are involved in lipid metabolism. Here, we analyzed the subcellular location of caveolin-1 in rat hepatocytes. The subcellular location of rat hepatocyte caveolin-1 was analyzed by cell fractionation procedures, immunofluorescence, and immuno-electron microscopy. Green fluorescent protein (GFP)-tagged caveolin-1 was expressed in rat hepatocytes. Lipid rafts were characterized after Triton X-100 or Lubrol WX extraction of purified peroxisomes. Fenofibric acid-dependent regulation of caveolin-1 was analyzed. Peroxisome biogenesis was studied in rat hepatocytes after RNA interference-mediated silencing of caveolin-1 and caveolin-1 knockout mice. Cell fractionation and microscopic analyses reveal that caveolin-1 colocalins with peroxisomal marker proteins (catalase, the 70 kDa peroxisomal membrane protein PMP70, the adrenoleukodystrophy protein ALDP, Pex14p, and the bile acid-coenzyme A:amino acid N-acyltransferase BAAT) in rat hepatocytes. Artificially expressed GFP-caveolin-1 accumulated in catalase-positive organelles Peroxisomal caveolin-1 is associated with detergent-resistant microdomains. Caveolin-1 expression is strongly repressed by the peroxisome proliferator-activated receptor-alpha agonist fenofibric acid. Targeting of peroxisomal matrix proteins and peroxisome number and shape were not altered in rat hepatocytes with 70%-80% reduced caveolin-1 levels and in livers of caveolin-1 knockout mice. Conclusion: Caveolin-1 is enriched in peroxisomes of hepatocytes. Caveolin-1 is not required for peroxisome biogenesis, but this unique subcellular location may determine its important role in hepatocyte proliferation and lipid metabolism. (HEPATOLoGY 2010;51:1744-1753.)