Rabbit Anti-Human SHC1 Polyclonal antibody

Three aerobic lignin-degrading bacterial strains were isolated from palm oil plantation soils. The bacterial isolates were screened using a selective nutrient medium of minimum salt media (MSM), with kraft lignin as lignin substrate and methylene blue as the ligninolytic dye indicator. The newly isolated bacterial strains SHC1, SHC2, and SHC3 were found to have the potential to tolerate high concentrations of kraft lignin and produced all three main ligninolytic enzymes (lignin peroxidase, manganese peroxidase, and laccase); these strains may therefore be useful in the degradation of lignin in oil palm empty fruit bunch biomass. The production of ligninolytic enzymes was carried out by means of submerged fermentation for 7 days using 2 mm of oil palm empty fruit bunch (OPEFB) fiber as a substrate. These bacterial isolates were characterized using biochemical tests from Biolog and identified using 16S rRNA gene sequencing analysis, which identified the strains SHC1, SHC2, and SHC3 as Bacillus sp., Ochrobactrum sp., and Leucobacter sp., respectively with 99% sequence similarity. Bacillus sp. SHC1 produced the highest manganese peroxidase (MnP) of 2313.4 U/L on the third day and the highest lignin peroxidase (LiP) of 209.30 U/L on the fifth day of fermentation. The optimum pH and temperature for the production of ligninolytic enzymes by Bacillus sp. SHC1 were pH 8 and 30 degrees C.

The amyloid precursor protein (APP) and its pathogenic by-product amyloid-beta protein (A beta) play central roles in Alzheimer disease (AD) neuropathogenesis. APP can be cleaved by beta-secretase (BACE) and alpha-secretase to produce APP-C99 and APP-C83. These C-terminal fragments can then be cleaved by gamma-secretase to produce A beta and p3, respectively. p3 has been reported to promote apoptosis, and A beta is the key component of senile plaques in AD brain. APP adaptor proteins with phosphotyrosine-binding domains, including ShcA (SHC1), ShcC (SHC3), and Fe65 (APBB1), can bind to and interact with the conserved YENPTY motif in the APP-C terminus. Here we have described for the first time the effects of RNA interference (RNAi) silencing of ShcA, ShcC, and Fe65 expression on APP processing and A beta production. RNAi silencing of ShcC led to reductions in the levels of APP-C-terminal fragments (APP-CTFs) and A beta in H4 human neuroglioma cells stably overexpressing full-length APP (H4-FL-APP cells) but not in those expressing APP-C99 (H4-APP-C99 cells). RNAi silencing of ShcC also led to reductions in BACE levels in H4-FL-APP cells. In contrast, RNAi silencing of the homologue ShcA had no effect on APP processing or A beta levels. RNAi silencing of Fe65 increased APP-CTF levels, although also decreasing A beta levels in H4-FL-APP cells. These findings suggest that pharmacologically blocking interaction of APP with ShcC and Fe65 may provide novel therapeutic strategies against AD.