[Latin Name]Huperzia serratum

[Source] Huperziceae whole herb from China

[Appearance]Brown to white

[Ingredient]Huperzine A

[Specification]Huperzine A 1% – 5%, HPLC

[Solubility] Soluble in chloroform, methanol, ethanol, slightly soluble in water

[Particle size] 80 Mesh

[Loss on drying] ≤5.0%

[Heavy Metal] ≤10PPM

[Pesticide residue] EC396-2005, USP 34, EP 8.0, FDA

[Storage] Store in cool & dry area, keep away from the direct light and heat.

[Shelf life] 24 Months

[Package] Packed in paper-drums and two plastic-bags inside.

[What is Huperzine A]

Huperzia is a type of moss that grows in China. It is related to club mosses (the Lycopodiaceae family) and is known to some botanists as Lycopodium serratum . The whole prepared moss was used traditionally. Modern herbal preparations use only the isolated alkaloid known as huperzine A. Huperzine A is an alkaloid found in huperzia that has been reported to prevent the breakdown of acetylcholine, an important substance needed by the nervous system to transmit information from cell to cell. Animal research has suggested that huperzine A’s ability to preserve acetylcholine may be greater than that of some prescription drugs. Loss of acetylcholine function is a primary feature of several disorders of brain function, including Alzheimer’s disease . Huperzine A may also have a protective effect on brain tissue, further increasing its theoretical potential for helping reduce symptoms of some brain disorders.

[Function] Used in alternative medicine, huperzine A has been found to act as a cholinesterase inhibitor, a type of medicine used to prevent the breakdown of acetylcholine (a chemical essential to learning and memory).

Not only used as a treatment for Alzheimer’s disease, huperzine A is also said to enhance learning and memory and to protect against age-related cognitive decline.

In addition, huperzine A is sometimes used to boost energy, increase alertness, and aid in the treatment of myasthenia gravis (an autoimmune disorder that affects the muscles).

Characterizing the DNA Damage Response by Cell Tracking Algorithms and Cell Features Classification Using High-Content Time-Lapse Analysis. Walter Georgescu et al (2015), PLoS ONE https://dx.doi.org/10.1371/journal.pone.0129438

Traditionally, the kinetics of DNA repair have been estimated using immunocytochemistry by labeling proteins involved in the DNA damage response (DDR) with fluorescent markers in a fixed cell assay. However, detailed knowledge of DDR dynamics across multiple cell generations cannot be obtained using a limited number of fixed cell time-points. Here we report on the dynamics of 53BP1 radiation induced foci (RIF) across multiple cell generations using live cell imaging of non-malignant human mammary epithelial cells (MCF10A) expressing histone H2B-GFP and the DNA repair protein 53BP1-mCherry. Using automatic extraction of RIF imaging features and linear programming techniques, we were able to characterize detailed RIF kinetics for 24 hours before and 24 hours after exposure to low and high doses of ionizing radiation. High-content-analysis at the single cell level over hundreds of cells allows us to quantify precisely the dose dependence of 53BP1 protein production, RIF nuclear localization and RIF movement after exposure to X-ray. Using elastic registration techniques based on the nuclear pattern of individual cells, we could describe the motion of individual RIF precisely within the nucleus. We show that DNA repair occurs in a limited number of large domains, within which multiple small RIFs form, merge and/or resolve with random motion following normal diffusion law. Large foci formation is shown to be mainly happening through the merging of smaller RIF rather than through growth of an individual focus. We estimate repair domain sizes of 7.5 to 11 µm2 with a maximum number of ~15 domains per MCF10A cell. This work also highlights DDR which are specific to doses larger than 1 Gy such as rapid 53BP1 protein increase in the nucleus and foci diffusion rates that are significantly faster than for spontaneous foci movement. We hypothesize that RIF merging reflects a “stressed” DNA repair process that has been taken outside physiological conditions when too many DSB occur at once. High doses of ionizing radiation lead to RIF merging into repair domains which in turn increases DSB proximity and misrepair. Such finding may therefore be critical to explain the supralinear dose dependence for chromosomal rearrangement and cell death measured after exposure to ionizing radiation.