Another possible way is ion exchange resin inkjet printed beads, i think i have heard of printed microfluicics and i have heard of 3D printed microfluidics, it might be possible to inkjet print digital gradients of ion exchange resin component chemicals,
then aim a warming laser to melt them so they bead up, then high frequency nonwarming pulse interval laser to stir them, making a digital gradient of different ion exchange resins responsive to a different chemical; a microfluidic channel layer is then
printed atop this (or previously beneath) and each of the separate ion exchange chemical concentrators has its own plumbing, at 32 micrometers radius of the bead then there are 47,851 chemically different chemical separation locations on a 7 cm times 7
cm chip

and possibly

or if 3D printing are printed on peltier cooled paper; or 72°F stable then they melt, liberating contents when a laser shines on them

Another way to make an IER chip is ion exchange resin inkjet printed beads, i think i have heard of printed microfluidics and i have heard of 3D printed microfluidics. It might be possible to inkjet print digital gradients of ion exchange resin component
chemicals, then aim a warming laser to melt them so they bead up, then high frequency nonwarming pulse interval laser to stir them, making a digital gradient of different ion exchange resin beads responsive to a different chemical; a microfluidic channel
layer is then printed atop this (or previously beneath) and each of the separate ion exchange chemical concentrators has its own plumbing, at 32 micrometers radius of the bead then there are 47,851 chemically different ion exchange resin chemical
separation locations on a 7 cm times 7 cm chip

Another way to make an ion exchange resin chip is

If you liquefy an ion exchange polymer with a laser or ambient warmth then use the actual multichannel microfluidics to transport the ion exchange polymer fluid to a particular well. It is it possible to fill 1 million different wells each with a
different chemical component ion exchange resin; blending liquid polymers, using microfluidics, at a variety of ion exchange resin chemical components that are blended together to make an array of 10,000 times 10,000 ingredient gradientized different ion
exchange resins, each of which will prefer to glom different chemicals than the other, doing that makes 100 million different ion exchange resins at a chip

It also makes me think this is a possible way to do what is effectively screening a library to find completely new ion exchange resin chemistries, if you then pump in the chemical you want to glom on an industrial scale, and have the microfluidic then
sequentially (parallel versions could work) liberate the glommed material you could find the most effective ion exchange resin composition out of 100 million (wells) which is likely much more efficient.

Niftily, ion exchange resins tuned to find chemicals of moderate electric charge and higher lipophilicity tend to concentrate the 100 million chemicals most likely to pass the blood brain barrier and omit macrophage and leucocyte response; that kind of
ion exchange resin chip could enrich the number of chemicals concentrated from the homogenate with chemicals that have more favorable drug characteristics which are then higher velocity at being turned into drugs

It could be possible to heighten ion exchange resting chemical concentration 11 times greater than wells with ion exchange resin fluid traversing sponge:

ion exchange resin highly porous sponge, blending saliva with rubber cement automatically makes a sponge so a chemistry of sponge making at microfluidic tube chambers could be straightforward, it is possible that rather than an ion exchange resin bead
well you would just make a higher volume tube volume of like a (========) filled with ion exchange resin sponge along the access plumbing microfluidic paths; think of a view like a circuit board multiparallelism with tube balloons periodically, the tube
balloons full of ion exchange resin sponge could have surface areas to the 3rd power causing them to glom with 32767 (32^3 micrometers) compared with (32^2 times 3 micrometers) at a well, that is near 11 times more material sorted at a similar surface
area but sponge hosting volume

If ion exchange resins can glom 1-10 pct of their volume of product, and 47,851

1/32,000 of a milliliter is the volume ofa 1 cm^2 area 32 micrometers deep, if the ion

1 cm cube that is 2/3 tubes concentrates 1-10 pct of chemical so .067 ml of concentrated material and can be used 11 times, so .67 ml of material

Compared with the 27 item multicuboid concentration and sortation reactor which is utilizes 27 cuboids, each 2/3 ion exchange resin sponge tubes, utilizable 11 to 140 timesreactor

Parallelism is beneficial at chemical sortation and chemistry chips, noting the 1 cm^2 two thirds of it being ion exchange sponge filled tubes product sorter and concentrator, When assembling a cuboid (like 27 packages stacked three on a side)
microfluidic chemical reactor or ion exchange resin cuboid form, a Lego (or better) interclick of perhaps 16 tubes per Lego circle thing to make a 27 times capacity reactor or product concentrator/sorter goes with having functional fluidic,and
microfluidic connection between the cuboids;

the actually fairly mild 16 times 6 circle tube fittings times 27 cuboids times 6 sides all surface Lego circle connectivity reactor would have 15.5k connections, perhaps better than brickle blocks is tHZ (or, just possibly at some polymers lasers like
the 3D shape deepwater laser scanner) weldable cube internals, so the up to 10k connections at a 27 cube Lego assemblable reactor (only about 10k connections out of 15.5k if you ignore the surface) could be Thz welded, puffed to fit, or even capped if
leaky, at a yield of just 95% 10,000 connector connectiviyy that produces 95% or higher functional plumbing access piping at the reactor multicuboid. The microfluidics at each cube could have some adaptive routing paths to make all the reactor/
concentrator well or tubes accessible. I think making these as spheres is also beneficial

The routing adaptive layer at the microfluidics makes it possible at a 27 cuboid reactor to route the chemical containing fluids clean withe reverse direction flow

Ion exchange polymer reloading as microfluidic pumping of new gradual chemical reaction to make new foam, laser or Thz

it is possible a soft flowing polymer with "brickle blocks with adaptive routing" could avoid the actually fairly mild 64 times 27 times 6 all surface Lego circle connectivity, perhaps better than brickle blocks is tHZ weldable cube internals, so the up
to 15.5k connections at a 27 cube Lego assemblable reactor could be welded, puffed to fit, or even capped if leaky, producing 95% or higher functional plumbing access piping at the Lego cube. I think making these as spheres is also beneficial



Integrated circuit technology microstructures; doing electrophoresis at microsized channels that are likely larger than the one million lane microfluidic chip I read about; An electrophoresis gel that is only a gel when it is cooled can be partitioned
and pumped around when it gently warms, although there is also the possibility of specific area of the chip warming with lasers; the many lane electrophoresis peltier cooled gel turns liquid at 16° then adjacent microfluidic lanes at 32 ° angles pump
the chemical or protein enriched fluid at just that area to a new location on the microfluidic chip; 1000 lanes are loaded at one side of each electrophoretic lane, so each electrophoresis lane at the chip can transport 1000 completely different
chemicals like proteins

There many ways to structure the microfluidic channels, some of them remind me of the connected and branching conductive lines on the upper surface of photovoltaic

Looks kind of like (→≠») or ==‡== where fluid flow direction meets a bunch of channels connected at an angle or #€[‡] other branched channel geometry

The liquid sample with liquid electrophoretic gel material that gels at 16°C loads at []‡ or ==‡== then peltier cools the multichannel ‡ to gel, then an integrated circuit, which just possibly is at the base of the electrophoresis chip if it is
made with integrated circuit technology as compared with polymer technology or MEMS technology, causes voltage at the long (‡)channels on =‡= causing the gel to sort chemicals, this can all be acvomplished with branches of branches at one layer, or,
layer atop ==== has another ==‡== fluid path on it; each concentration at the gel channel can be liquified with lasers; microfluidics utilizes published pumps so above 16° C when the === areas when the concentrated chemical are liquid they are micro
fluidically motionized to the perimeter of the chip for further use, alternatively they can just be micro fluidically transported to where the yeast are; at another version the microfluidics transport the electrophoresis products to a bunch of wells on a
multimillion well integrated circuit technology like planar area, and then to place the yeast and nutrients, the mechanisms automatically, or if feeling thrifty, a human gently places, or possibly even mists the multimillion well plate that has the
plurality of separate concentrated chemicals that the microfluidics have placed at predictable locations and at a database, the actual yeast and nutrient solutio; the wells have the volume capacity to feed yeast for 20 unmedicated yeast lifespans noting
that yeast now can be made to live 400% longer (salicylic acid) so that way if the 99.999th percentile of longevizatiom causes a lot of yeast longevity they will have nutrients the entire time.

It is possible putting the entire thing on an ultrasonic transducer will heighten fluid diffusibility

To produce a larger amount of chemicals, utilize some other channel sizes, make the multichannel integrated circuit technology electrophoresis chemical concentrator produce 100 MCG of product per each second or third branch (or layer) of sequentially
purer electrophoretic ==‡== channels, 1000 or 10,000 ==‡== functioning in parallel, loaded from the sides of chip with larger distributive microfluidic |[]| perimeter channels, provides higher volume of material being concentrated; there are 2500
preconcentration material loader channels on each perimeter side; 100mcg times 10,000 ==‡== channels processes 1000 mg, 1 gram of sample each full cycle, at 20 minutes per cycle then 72 grams of sample can be separated per day, 14 of these chips
stacked in parallel can process and purify 1 Kg per 24 hours



If a yeast weighs a microgram, and it is possible there is a yeast species that massive (1 million yeast per gram) then dosing the yeast at the human equivalent of 2 grams to 1 micrograms human equivalent dose with the chemicals concentrated at a
microfluidic electrophoresis chip is possible

Notably having millions of wells at an integrated circuit wafer technology or even MEMS polymer form makes the amount of locations so the yeast can be dosed at numerous different orders of magnitude, about 7 orders of magnitude between 2 grams (phenibut)
and 600 nanograms (ethynyl estradiol) human equivalent dose at 8 wells of yeast each to get p value

What if the microfluidic chemical sorter had 100 micrometer channels, and 100 of them on each perimeter side that are moving preconcentrated material at each perimeter side of the chip, well that perimeter is a surface area kind of like one cm^2 of
motionized fluid; Depth: at 100 micrometers of 16°C electrophoretic liquifiable depth, and 11 minutes per cycle to traverse up to .5 cm (before branching) while having 10,000 micro fluidically addressable tube segment tapping branches (noting the 1
million microfluidic lane chip I read about) then it is like a volume of 1/100th of a ml each 11 minutes or about 1.3 ml per 24 hours. A 7 cm^2 version would produce 63.7 ml of 10,000 sorted chemicals. If less specific lengths of the liquified
electrophoretic lane tapping tubes were utilized then you could get larger amounts of 1000 chemical fractions, at 63.7 ml that is 63.7 mg of each of the 1000 different chemicals, although it is actually different than that from solvent mass, so 6.3 to 32
mg per 24 hours could be from 90-49% liquigel solvent

The thing being that the person is producing mg or more of a longevity drug to characterize and quantify at 6 month 96 well plate fish or mice,

If 1 out of every 1000 or 10,000 (different chemical quantities from different resolutions that make .63 to 6.3 mg of concentrated chemical to dose organisms with)

That makes 10,000 or 1000 microfluidic branched channel electrophoresis concentrates, of different numbers of simultaneous chemicals from few or even one to ten times as many from ultrasonicated endolith homogenate. These 1000 or 10,000 chemicals could
then be screened knowing, kind of, what they are. Also the microfluidic chip could have 10,000 wells on it so an eentsy sample could be removed if really precise characterization is the thing to do. The amounts, going with the convenient unrealistic
presumption of 1000 chemicals of equal amounts is sufficient to dose a mouse with a multidays of dose produced every 24 hours, or at 10,000 chemicals, c elegans. The c elegans could be dosed throughout its life from one 24 hour output. This is

A way to make 99.99th percentile of longevizing chemicals at 24 hours. If age batched c elegans were used for testing then 6 or 9 days would produce a longevity increase %.

Finding the longevity drugs:Use microfluidics to connect the multimicrochannel electrophoresis chemical separator to 100 million yeast colony wells or 100 million human tissue colony wells then use the: the more GFP it produces the longer it has lived
varieties of yeast or human tissue culture cells, these emit more light the longer they live then have camera note the most light emitting cells at wells,

It is possible that finding a most longevizing chemical from half a billion different chemicals longevity drug chemical could cause a person to systematically follow twig to branch on a half billion leaf treeee, possibly doing all 29 Binary experiments
to find the identity of the chemical. exposing yeast to half a billion different chemicals, then utilizing flow cytometry to find the one with the greatest light emission tells that if it turns the yeast into anendolith lifespan longevity organism it is
beneficial to test it on mammals and give it to humans;

Utilizing liposomes with, approximately, just one chemical at them to quantify and characterize new longevity drugs:

With the possibility that a continuum gradient electric charge or pH gradient generation around liposomes, causing them to ensconce different things (or putting phosphatidyl serine and alcohol at an electrophoresis gel that liquefies above 16°C then
beaming ultrasonics on the phosphatidyl containing gel produces liposomes to form right there, at a micrometer or eentsier sized piece of a chemical/protein band, ensconcing just that location's chemicals at that electrophoresis band generates a billion
or a trillion liposomes, each with mostly just one particular chemical;

You blend the one-liposome-one-chemical liposomes with a one yeast one liposome dilution at a container of fluid, or possibly decanted to make a monolayer; longevity chemicals make the yeast live longer and the most fluorescent yeast has lived the
longest, the longest lived 700 yeast are detected with 20 million yeast per second flow cytometry and a numeric characterization of that entire library like endoliths or the kings holly can be made. finding something that makes yeast live numerous orders
of magnitude longer and noting flow cytometry lets the yeast live on, many of the yeast remain alive

Then there is a way to trace the long lived yeast to the liposome it ate, and the chemical at the liposome; it has to do with the sensitivity of isotope spectroscopy at flow cytometry, the liposomes can have a large location specifying dose of stable
isotopes at them because the electrophoresis gel either migrates a gradient of isotopes with 2-6 different isotopes migrated from each distal part or face of the gel before electrophoresising the screenized material like kings holly or endoliths; so the

isotope gradient, deuterium from one distal part, nitrogen from the other distal part, phosphorus from a transverse side and oxygen from another transverse side; each liposome also then gathers a region associated multiisotope ratio at amounts that can
be seen with spectrophotometry of the yeast at the flow cytometer if that narrows the content of the liposome to an eentsy area of the electrophoretic gradient distance (microfluidic is micrometers) then the name of the source and its library of congress
number is known and then the process is repeated to find the page paragraph the particular chemical molecule is on.

Microfluidic version, transport numerous nearly identical electrophoretic liposomes sequentially to the yeast upping isotope dosage two or three orders of magnitude, and heightening actual chemical dose.

Liposomes are make able at different volumes, it is possible that liposomes with 300 times more dosing chemical are valued or possibly really eentsy liposomes with higher chemical/spatial resolution are valued.

possible then when a trillion liposomes form there could be a billion liposomes amongst those that had mostly just one kind of chemical or molecule, the one near them on an electrophoretic band that could be ensconced into a liposome at just that minute
variation in isoelectric point, pH, p(some other chemical like NH3) (pNH2), so with a trillion gradient formed liposomes you get a billion mostly one chemical liposomes, (even though only a billion of them are highly focused)

Then After dipping, rinsing, liposome surface reacting, the liposomes with something like ribose or something yeast like to eat, put them at a dilution fluid so the ratio of liposomes to yeast is one liposome to one yeast; the yeast eats the liposomes
then You can tell if the liposomes chemical longevizes because things like known longevity drug liposomes make their individual yeast live longer, and the liposomes volume and appetizing coating can be adjusted to get the highest ingestion and
longevization response

Does this work with daphnia; could you laser zap an isotope gradient preloaded then longevity drug electrophoresisized gel to make eentsy 11 micrometer sized daphnia food cuboids, then feed them to daphnia to characterize and quantify the longevity
effects, doing flow cytometry with spectrophotometry to find the isotopes that describe the location on the electrophoresis gel which tells which chemical book I'd or neighborhood it is from; daphnia are possibly a better longevity quantification
organism than yeast.

Could isotope labelled electrophoretic liposomes screen billions of potential antibiotics rapidly, the bacteria that eat the liposomes with the most powerfully antibiotic fluotesce the least when all the nonliving bacteria are orocessed at the flow
cytometer. new antibiotics save lives

Grow a sprig of the king's holly in isotopically labelled water, or perhaps do gene therapy on it with isotope labelled DNA, or provide it with isotopically labelled amino acids, or do all three with different stable isotopes; then do electrophoresis
like microfluidic electrophoresis or bulk liposomal electrophoresis then when the flow cytometer spectrophotometric thing detects isotopes it is detecting them on actual longevity chemicals



It is possible that some drugs or other chemicals have very high area localization at the brain or body as they are, but that nobody knows of any illness linked to that highly reachable mapped area. Based on how it would likely function to attach
another molecule, a drug, to the chemical that reaches that map area they could research the highly reachable areas to find out if adjusting their function would benefit humans, anything from actual medical treatment to causing the highly reachable areas
to be what I have read is called better than well

Localization mental illness drugs, keep anti psychotics out of sleepiness areas if they still function

People create ways to keep protein from gunking up tubes, it is possible that unlike proteins, peptides, which can also be drugs, have chemical things which make them much easier to keep ungunkifying, from being able to clean all the peptides off of them
off with an enzyme, possibly a deaminase, to drastically fewer gooey nooks at the molecule from having masses and structures up to hundreds of thousands of times less complex, it is possible that peptides screened (or produced) at microfluidics are easy
to keep from gunking up areas, surfaces, connectors and geometries that accumulate material, microfluidics technologies at peptides could be clean, fast, durable, and with longer reliability cycles; screening libraries of peptides as longevity drugs with
1/1000th the gunkification at chips could heighten reusability which makes, concentrating, sorting natural peptides better, also absent gunkification the thousands more uses per chip makes it hundreds of times more affordable. From the perspective of
making drugs and molecules that benefit people the 2019AD also noting the combinatorial space of peptides is kind of like many factorial and new completely artificial amino acids for peptides have been created, so it is a nonfinite factorial there could
be a multihundred times better ungunkiness, tidiness, rinsability at peptide sorting and concentrating chips.

Some peptide libraries that could be mass screened for new longevity drugs: if you divide any protein into pieces about half a hundred amino acids long or eentsier it becomes a peptide so any longevity causing proteins could be made into pieces and
screened at yeast in the billions (flow cytometry characterizes 10 billion yeast a second) so if the yeast are engineered to make and accumulate more green fluorescent protein the longer they live, it is possible to find out which yeast have the greatest
longevity increase. Longevity proteins could be things like naked mole rat organ homogenate, any electrophoretic band that is at 35 year beavers compared with mice, any electrophoretic band from voluntarily provided, or not-alive person protein
differences between humans and other primates, protein bands from termite queens (50- I read, 100 year longevity) not at other termites, the protein band differences between the 17 year part of the cicada's phenotype and its one month long mating form,
queen bees and regular bees, the longest lived non s cerevisia yeast and s cerevisia and the briefest yeast, electrophoretic protein bands at the kings holly, 40,000 year lifespan thus far, with the protein not at a few other plants, protein bands at
endoliths of numerous species (fungi, algae, cyanobacteria, bacteria) electrophoretic that are not at similar organisms, also noting whale longevity the electrophoretic protein bands at 214 year old whale tissue from non alive whales, or 214 year whale
tissue from parturition related tissue in the water, that are absent from other whales; note that there are numerous others and that just these 22 could be macroscopically electrophoresized to get 10-1000 micrograms to dose the yeast with.

Also it would be beneficial when generating the peptides, rather than using enzymes, or even a many enzymes at one flask approach, to divide the proteins into peptides at nonpredictable locations because if you always use an enzyme that divides with
lysine then the peptides will all have a distal lysine on them, one possibility is UV radiation, other radiation, or bubbling O3 through the flask

Spectroscopy of isotopically labelled peptides, would a spectroscopy beam at a flow cytometer looking at a yeast be able to see femtograms or picograms of radio labelling from a peptide at the yeast, perhaps, perhaps not, what about a one per 100,000
likeliness of seeing the isotopic labelling and the 20 million yeast per second flow cytometer I read they thought they could make, then that is 200 yeast saying which peptide they have been dosed with per second then that is 630.7 million peptides
screened annually, with parallel machines, like 11 of them, that is 69 billion peptides screened for longevity effects. There are 2 1/2 longevity peptides out of that I have heard of, so at an extreme, 1 million published peptides so they might find some
from a million isotopically labelled peptides that the first 14 days of spectroscopic flow cytometry of yeast finds, and the flow cytometry of fluorescent proteins notes have highest longevity increase. They could then utilize about 11 96 well plates of
c elegans or 6 month fish to quantify the effects on vertebrates of the most longevizing 132 of the peptides.

Use peptide sequencers, and if there are microfluidic peptide sequencers, noting the million channel microfluidic chip i read about, creating combinatorial peptides based on software, like AI, like deep learning AI that predicts effective longevity
increase and then makes those longevity peptides which are screenable at yeast.



Precluding protein gunk up at microfluidics, at something like fungal or algal endolith homogenate longevity chemical screening or clam homogenate longevity screening with numerous proteins at the ==‡== microfluidic microelectrophoretic sorter could
direct each concentrated, separately tapped band of material at the gel to a microfluidic lane that has an interior polymer (or other material) surface charge that minimizes protein accumulation on the channels sides, at that particular protein's actual
characteristics, kind of since you know the charge it is at and responds to you can have it traverse channels where that channel's interior charge is neutral or slightly surface-diffident whichever causes less gunking up

Longevity technology: AEDG (Epithalon) is a peptide published as causing 24% greater longevity at mice, and when administered with thymosin, it makes people 4 times more likely to be alive after 6 years; there are now synthetic amino acids they make, so
molecular variants of the A, E, D, G amino acids that are synthetic could be made, assembled into new versions of epithalon and quantified as to longevizing effects; with two new atom swapouts or new atoms per each new synthetic amino acid, that is just
16 binary variants to screen at mice, yeast or human tissue culture, notably this provides a kind of nifty rapid research utilizing human cognition originated drug creation. Noting using a D-amino acid is part of how vasopressin was modified to be orally
active a person could enjoy, like, and value making an orally available D amino acid or synthetic amino acid version of Epithalon. Like if I were making a variation, thinking as a human, I would find out if acetylated synthetic amino acid variations on
any of the amino acids in AEDG were previously existing, then distal to the part of other things Epithalon they might think Epithalon attaches to or activates things with, I would put the acetylated synthetic amino acid because I think it might cause the
acetylated amino acid version of Epithalon to pass the blood brain barrier more effectively, predictably, or pre looking things up online I would find out if achiral (nonchiral) synthetic amino acids have been produced (imaginably a dimer, even like the
G at AEDG being doubled, a new achiral glycine)

If this were at a public biotechnology maker space like they have in San Francisco and New York City then it would be nifty to have each of 7 or 14 people each think of their own version of AEDG with the makerspace maker shared enthusiasm and actual
craft of making, although possibly just ordering (another pineal gland peptide distally attached to AEDG might have synergistic longevity effects, causing greater longevity increase at mice than the published 24%) things. Also if people at the makerspace
knew about AI, or even just the deep learning packages they have, then one of the makerspace people could make a computer program that uses deep learning to create AEDG variation molecules, as well as other longevizing molecules and enjoy doing that, as
well as of course wondering how well it would do compared with the human originated versions. If AEDG has a longevity effect on c elegans or more beneficially 96 well plate 6 month fish, then 3 of these plates would give results on the 7-14 people's AEDG
versions times 2 or more variants each, utilizing 8 organisms to get a p value, that is 224 wells of fish as well as c elegans to quantify all 14-28 variations.

There is also screening a library to find a more longevizing version of epithalon, from a synthetic amino acid perpective, Modifying the four amino acids to have four atom swapouts per amino acid then that is 2^16 screenable variants, near 65,536
versions; going with the idea they could modify the Epithalon on purpose they could make eight atom swaps or additions each at the two amino acids on the side of epitalon that actually activates things (if there is a receptorside, make the two groups of
four atom swaps at the receptorside) then these 65,536 could be screened at yeast as well as human tissue culture to find 99.9th percentile of greater longevity increase from the molecules screened. I do not know if Epithalon makes c elegans as well as
daphnia live longer or not, if it does then these could be utilized to compare different AEDG, Epithalon variants.

I perceive Epithalon might be tolerated at a multi-order of magnitude dose range, if it is then that suggests something Epithalon activates gets fully activated, kind of saturated; finding out what that saturated thing is, then making more of the
saturated thing, or possibly supplementing, as a longevity drug, the amount of the saturated thing could be a new longevity drug; also i do not know if the saturated thing is a cell type, a receptor at the brain (CNS) and at many places at the body, or a
chemical. If it is a cell type or receptor then the genetics of the saturated thing like SNPs, alleles, or copy number variations could be part of the genetics of greater longevity; if it is a cell type or receptor then the epigenetics that effect the
amount of DNA transcription that effect how frequently or how many of that receptor gets made could be longevity heightening epigenetics, some epigenetics effects function at multiple generations of humans so it is actually possible taking a tuned HDAC
inhibitor could turn making lots more of the saturated thing on, or make lots more of it, and that the heightened longevity effect transfers to your children and grandchildren.

Does making BDNF nerve growth factors or other growth factors at the pineal gland heighten longevity and healthspan.

Other pineal hormones, Epithalon, to my perception was developed from researching pineal peptides, it is possible some of the other pineal peptides are more longevizing but at the time a four amino acid quadropeptide was particularly easy to purify and
make, it is possible there are lengthier amino acid sequence pineal peptides that can now simply be ordered to be constructed online and screened at mice to find out if they have greater longevizing effects than Epithalon

Does a 300 year lifespan tortoise have a pineal gland? What about a century bird lifespan bird, could a recently alive, hospice-care like administered multicentury lifespan whale's pineal gland have its peptides sequenced, all of these pineal peptides
could be tested at mice to find out if they are heighten longevity above epithalon's published 24%


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