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Basic guide to using CJC-1295 & GHRP-6

What is growth hormone?




Synthetic Growth Hormone is an artificially created hormone “identical” to the major naturally produced (endogenous) isoform. It is often referred to by its molecular mass which is 22kDa (kilodaltons) and is made up of a sequence of 191 amino acids (primary structure) with a very specific folding pattern that comprise a three-dimensional structure (tertiary structure). This tertiary structure is subject to potential shape change through a process known as thermal denaturation. While many labs are capable of generating growth hormone (GH) with the proper primary structure not all will be capable of creating a tertiary structure identical to the major naturally occurring growth hormone. The tertiary structure can determine the strength with which the growth hormone molecule binds to a receptor which will in turn affect the “strength” of the intracellular signaling which mediates the events leading to protein transcription, metabolism, IGF-1 creation, etc. It is this inconsistency that accounts in part for the differences in effectiveness of various non-pharmaceutically produced synthetic growth hormone.

Naturally produced Growth Hormone is produced in the anterior pituitary and to a far lesser extent in peripheral tissue. It is made up of a blend of isoforms the majority of which is the 22kDa (191 amino acid) variety with which most are familiar. In addition an isoform that is missing the 15 amino acids that interact with the prolactin receptor is also produced. This form is known as 20kDa and although it binds differently to the growth hormone receptor it has been shown to be equally potent to 22kDa. It appears that 20kDa has lower diabetogenic activity then 22kDa. The pituitary releases a blend of these two isoforms with 20kDa averaging perhaps 10% of the total although this percentage increases post-exercise. Currently there is no synthetic produced for external administration for this isoform.

Growth hormone (GH) in the body is released in pulsatile fashion. It has been demonstrated that this pattern promotes growth. The pituitary is capable of rather quickly synthesizing very large amounts of growth hormone which it stores large amounts in both a finished and unfinished form. Adults rarely experience GH pulses (i.e. releases of pituitary stores) that completely deplete these stores. As we age we do not lose the ability to create and store large amounts of growth hormone. Rather we experience a diminished capacity to “instruct” their release. The volume of GH that is released can not be properly equated to the exogenous administration of synthetic GH for the reason that a set of behavioral characteristics accompany natural GH that differ from those of synthetic GH. Among those characteristics are concentrated pulsatile release which upon binding in mass to growth hormone receptors on the surface of cells initiate signaling cascades which mediate growth events by translocating signaling proteins to the nucleus of the cell where protein transcription and metabolic events occur.

These very important signaling pathways desensitize to Growth Hormone’s initiating effects and need to experience an absence of Growth Hormone in order to reset and be ready to act again. The presence of GH released in pulsatile fashion is graphed as a wave with the low or no growth hormone period graphed as a trough. Therefore attempting to find a natural GH to synthetic GH equivalency is not very productive because in the end what is probably import is:

- the quantity & quality of intracellular signaling events; and
– the degree to which GH stimulates autocrine/paracrine (locally produced/locally used) muscle IGF-1 & post-exercise its splice variant MGF.
Synthetic GH versus Natural GH in IUs

An attempt has been made on my part and can be found at:

#8 – Growth Hormone Administration vs. CJC-1295/GHRP-6 + GHRH (part I of II)

#9 – Growth Hormone Administration vs. CJC-1295/GHRP-6 + GHRH (part II of II)
Rather than demonstrate absolute values this comparison articles should serve to demonstrate that the body can produce pharmacological levels of growth hormone.

Brief overview of natural GH release

The initiation of growth hormone release in the pituitary is dependent on a trilogy of hormones:

Somatostatin which is the inhibitory hormone and responsible in large part for the creation of pulsation;

Growth Hormone Releasing Hormone (GHRH) which is the stimulatory hormone responsible for initiating GH release; and

Ghrelin which is a modulating hormone and in essence optimizes the balance between the “on” hormone & the “off” hormone. Before Ghrelin was discovered the synthetic growth hormone releasing peptides (GHRPs) were created and are superior to Ghrelin in that they do not share Ghrelin’s lipogenic behavior. These GHRPs are GHRP-6, GHRP-2, Hexarelin and later Ipamorelin all of which behave in similar fashion.
In the aging adult these Ghrelin-mimetics or the GHRPs restore a more youthful ability to release GH from the pituitary as they turn down somatostatin’s negative influence which becomes stronger as we age and turn up growth hormone releasing hormone’s influence which becomes weaker as we age.

The exogenous administration of Growth Hormone Releasing Hormone (GHRH) creates a pulse of GH release which will be small if administered during a natural GH trough and higher if administered during a rising natural GH wave.

Growth Hormone Releasing Peptides (GHRP-6, GHRP-2, Hexarelin) are capable of creating a larger pulse of GH on their own then GHRH and they do this with much more consistency and predictability without regard to whether a natural wave or trough of GH is currently taking place.

Synergy of GHRH + GHRP

It is well documented and established that the concurrent administration of Growth Hormone Releasing Hormone (GHRH) and a Growth Hormone Releasing Peptide (GHRP-6, GHRP-2 or Hexarelin) results in synergistic release of GH from pituitary stores. In other words if GHRH contributes a GH amount quantified as the number 2 and GHRPs contributed a GH amount quantified as the number 4 the total GH release is not additive (i.e. 2 + 4 = 6). Rather the whole is greater than the sum of the parts such that 2 + 4 = 10.

While the GHRPs (GHRP-6, GHRP-2 and Hexarelin) come in only one half-life form and are capable of generating a GH pulse that lasts a couple of hours re-administration of a GHRP is required to effect additional pulses.

Growth Hormone Releasing Hormone (GHRH) however is currently available in several forms which vary only by their half-lives. Naturally occurring GHRH is either a 40 or 44 amino acid peptide with the bioactive portion residing in the first 29 amino acids. This shortened peptide identical in behavior and half-life to that of GHRH is called Growth Hormone Releasing Factor and is abbreviated as GRF(1-29).

GRF(1-29) is produced and sold as a drug called Sermorelin. It has a short-half life measured in minutes. If you prefer analogies think of this as a Testosterone Suspension (i.e. unestered).

To increase the stability and half-life of GRF(1-29) four amino acid changes where made to its structure. These changes increase the half-life beyond 30 minutes which is more than sufficient to exert a sustained effect which will maximize a GH pulse. This form is often called tetrasubstituted GRF(1-29) (or modified) and unfortunately & confusingly mislabeled as CJC-1295. If you prefer analogies think of this as a Testosterone Propionate (i.e. short-estered).

Note that some may also refer to this as CJC-1295 without the DAC (Drug Affinity Complex).

Frequent dosing of either the aforementioned modified GRF(1-29) or regular GRF(1-29) is required and as previously indicated works synergistically with a GHRP.

In an attempt to create a more convenient long-lasting GHRH, a compound known as CJC-1295 was created. This compound is identical to the aforementioned modified GRF(1-29) with the addition of the amino acid Lysine which links to a non-peptide molecule known as a “Drug Affinity Complex (DAC)”. This complex allows GRF(1-29) to bind to albumin post-injection in plasma and extends its half-life to that of days. If you prefer analogies think of this as a Testosterone Cypionate (i.e. long-estered)

CJC-1295 is difficult to produce and expensive to make. As a result it could be cost-prohibitive to use extensively. Modified GRF(1-29) while less convenient is much less expensive to make and because it is a pure peptide the synthesis process is straightforward. It should sell at a fraction of the cost of CJC-1295.

written by DatBtrue

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Peptide Guide Information

Peptides come in the form of lyophilized (freeze dried) powder. The amount of powder/product is stated in International Units (IU’s) or in Milligrams (MG).
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Melanotan peptides (Melanotan 1 & Melanotan 2), PT-141 Bremelanotide, GH Fragment, Ipamorelin, CJC-1295 & GHRPs (GRHP-2 & GHRP-6), HGH, HCG, et cetera use Bacteriostatic Water (BW). Bacteriostatic Water for injection, USP is a sterile, nonpyrogenic preparation of water for injection containing 0.9% of benzyl alcohol added as a bacteriostatic preservative. It is supplied in a multiple-dose container from which repeated withdrawals may be made to dilute or dissolve drugs for injection. The pH is 5.7 (4.5 to 7.0)

For IGF use an acetic acid solution (.6%) which is 7 parts distilled water and 1 part vinegar to reconstitute. You must filter the distilled water and white wine vinegar through a sterile 20 micron syringe filter before use. Sodium Chloride (NaCl) is used to buffer the injection.

1.) Take an alcohol swab to the stopper of both your peptide vial and the vial of the dilutent.
2.) Draw your preferred dilutent (BW) with a 1cc syringe. Choose an amount that will make measuring the final product simple.
1ml(cc) per 10 mg vial of Melanotan would mean each 10 tick marks on a U100 slin syringe would equal 1mg of Melanotan
1ml(cc) per 10 IU vial of HGH would mean each 10 tick marks on a U100 slin syringe would equal 1 IU of HGH
3.) Take the syringe with the dilutent and push it into the vial of lyophilized powder letting the dilutent dissolve the peptide. Many (not all) peptides are sealed with vacuum pressure, be careful
4.) After dilutent has been added to the vial, gentling swirl the vial until the lyophilized powder has dissolved and you are left with a clear liquid. The peptide is now reconstructed, ready for measurement and usage.
5.) Store your now reconstituted research peptides in the refrigerator.

Peptide Measurement
After successfully reconstituting your peptide, measure the desired amount out for injection. Use a U100 insulin syringe to draw out and inject your product.

Since you know the amount of IU’s/MG’s in your vial, we divide this out as follows:
You will need to know the following to be successful: 1ml = 1cc = 100 IU’s

We take our dose from the label of the dry lyophilized powder and we divide that into the amount of dilutent used.

Example- We used 1cc(ml) of water. We have a 10 IU vial of HGH.
From our formula above we know that 1cc = 100 IU’s, so we have 100 IU’s of water.
We now divide the 100 IU’s (the amount of our water) by 10 IU’s (the amount of our HGH)
100 IU / 10 IU = 10

This 10 will perfectly correspond with the markings on a U100 insulin syringe. In our example every 10 mark on our syringe will equal 1 IU of HGH. Want to draw out 2 IU’s of GH? ….draw out to the 20 mark on the syringe (1/5th of the syringe).

Say you have a 1mg vial and you add 1ML you get
1000mcg/1mL: 10 mcg per IU
1000mcg/2mL: 5 mcg per IU




Say you have a 10mg vial and you add 1ML you get
10mg/1mL: 1 mg per 10 IU
10mg/2mL: .5 mg per 10 IU

Say you have a 20mg vial and you add 1ML you get
20mg/1mL: 2 mg per 10 IU
20mg/2mL: 1 mg per 10 IU

Say you have a 10iu vial and you add 1ML you get
10iu/1mL: 1 iu per 10 IU (on the syringe – 1/10th the product)
10iu/2mL: 1 iu per 20 IU (on the syringe – still 1/10th the product)
Say you have a 5000iu vial and you add 1ML you get
5000iu/1mL: 500iu per 10 IU
5000iu/2mL: 250iu per 10 IU

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