Growth Hormone Releasing Hexapeptide (GHRP-6)
Peptide Sequence: His-D-Trp-Ala-Trp-D-Phe-Lys-NH2
Molecular Formula: C46H56N12O6 Molar Mass: 873.014 g/mol CAS Number: 87616-84-0
GHRP-6 5mg
Growth Hormone Releasing Peptide 2
Peptide Sequence: H-D-Ala-D-2-Nal-Ala-Trp-D-Phe-Lys-NH2
Molecular Formula: C45H55N9O6 Molar Mass: 817.9 g/mol CAS Number: 158861-67-7
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Important Notification: All of our products and services listed in this website are for research or production use only, not for direct human use.
The hexipeptide GHRP – 6 is a secretagogue peptide that has a molecular formula of C46H56N12O6and a molecular weight of 873.014. Its structure is comprised of six amino acids. The name of the peptide itself is an acronym that stands for Growth Hormone Releasing Peptide.
GHRP – 6 and the Pituitary Gland
Scientific study that has been based on animal test subjects has determined that the way in which GHRP 6 has been shown to function chiefly ties into its relationship with the pituitary gland; the tiny, pea-sized gland that is located at the bottom of the hypothalamus at the base of the brain. In essence, this gland is charged with the regulation and control of a host of different processes that are tied to the endocrine system. Some of these processes include metabolism, thyroid gland functionality, temperature regulation, internal water regulation, pain relief, and growth. GHRP – 6’s overall functionality is such that it inhibits the pituitary gland from blocking the production of secretions that directly tie to these regulatory processes. This then allows for the animal test subject to have the ability experience a more efficient means of achieving a level of homeostasis in regards to these regulatory processes.
GHRP – 6 and the Stomach
It has also been determined by scientific study based on animal test subjects that GHRP – 6’s overall functionality can be linked to the production of ghrelin. In essence, ghrelin is an amino acid that is primarily produced by the cells that line the stomach, although it has been noted that it can also be secreted by the epsilon cells that are found in the pancreas. The expression of this particular secretion serves to stimulate the sensation of hunger; this allows it to act as a counterbalance to amino acid leptin, whose secretion stimulates the sensation of feeling full. Studies have indicated that GHRP – 6’s functionality allows for a greater level of ghrelin to be produced. This extra level of production prolongs the amount of which an animal test subject can experience hunger. This in turn enables the test subject to intake a greater amount of food which can then be used as fuel for the pituitary gland’s elevated ability to secrete endocrine system-related expressions.
GHRP – 6 and the Liver
Further scientific study that has been based on animal test subjects has determined that GHRP – 6’s abilities have a connection with the liver; specifically, with a liver-based secretion known as Insulin-like Growth Factor-1, or IGF-1. This secretion has been shown to be highly reactive in nature, meaning that its expression has been tied to the growth and repair of muscle and tissue growth. Studies have indicated that GHRP – 6 has the capacity to influence an elevated production amount of this particular secretion, thus allowing an animal test subject a more efficient rate in achieving homeostasis on a muscular and skeletal tissue level.
GHRP – 6 and the Central Nervous System
It has also been determined through scientific study based on animal test subjects that the presence of GHRP – 6 aids in the activation of intracellular signaling pathways along the central nervous system; these pathways are ones that are used by various secretions that are tied to the pituitary gland. Additionally, it has been shown that it has the ability to promote a greater level of protein expression in terms of overall cellular survival. These functions have led to the determination that it could be a prime ally in the guarding against cell loss and functionality in the aftermath of a hypoxic-ischemic brain injury, such as:
- Stroke
- Angina Pectoris caused by cardiac arrest
- Angina Pectoris caused by respiratory arrest
Various Elevated Processes
Because of the way in which GHRP 6 has been shown to function, scientific study that has been based on animal test subjects has been able to determine that its presence can be responsible for several elevated processes. These processes have been thought to include an increase in muscle growth, a decrease in body fat, an elevation in muscle and tissue repair, an expedited rate of recovery from injury, a boost in bone density, increased immune system efficiency, and a boost in connective tissue and joint strengthening.
Strictly for Controlled Environments
It should be noted that any findings or observations that relate to GHRP – 6 and its overall functionality should exclusively be done within a strictly controlled environment, such as a medical research facility or a laboratory. The reason for this is due to the fact that the peptide and the study its operational is currently just fit for scientific study on animal test subjects. As such, it should be noted that research that has been derived regarding GHRP – 6 is due to scientific tests conducted in a controlled environment only.
Sequence: PEG-Tyr-Gln-Pro-Pro-Ser-Thr-Asn-Lys-Asn-Thr-Lys-Ser-Gln-Arg-Arg-Lys-Gly-Ser-Thr-Phe-Glu-Glu-Arg-Lys-NH2
Molecular formula: C121H200N42O39
Molar Mass: 2888.16
CAS number: N/A
Synonyms: Pegylated MGF, PEG IGF-1 Ec
PEG MGF is a splice variant of the IGF produced by a frame shift if the IGF gene and PEGylated to improve stability. PEG-MGF, or PEGylated Mechano Growth Factor, is a new and innovative form of the IGF produced by a frame shift if the IGF gene, namelyMechano Growth Factor (MGF), which is PEGylated to improve stability that outperforms natural MGF many times over. MGF is a splice variant of the IGF gene which increases stem cell count in the muscle and allows for muscle fibers to fuse and mature. This is a process required for growth of adult muscle. Natural MGF is made locally and does not travel into the bloodstream. Synthetic MGF is water based and when administered intramuscularly, travels into the bloodstream. MGF is only stable in the blood stream for only a few minutes. Research has shown that PEG-MGF helps increase the muscle stem cell count, so that more may fuse and become part of adult muscle cells.
What is the Pegylation of Mechano Growth Factor?
PEGylation is the act of attaching a Polyethylene glycol (PEG) structure to another larger molecule (in this case, MGF). The PEG acts as a protective coating and the theory here is that this will allow the MGF to be carried through the blood stream without being broken down. Neurological research has shown that utilizing PEGylated MGF resulted in a longer more stable acting version of the MGF peptide in serum/blood.
The Effects of Pegylated MGF
Mechano Growth Factor (MGF) exhibits local effects in skeletal muscle and without cannot travel through the body without modification. The problem with synthetic Mechano Growth Factor (MGF) is that it is introduced intramuscularly and is water based so it goes into the blood stream. When used this way, Mechano Growth Factor (MGF) only remains stable in the blood stream for a few minutes. Biologically produced MGF is made locally and does not enter the bloodstream. It is also short acting so stability is not an issue. By PEGylating the Mechano Growth Factor (MGF) it is almost as efficient as local produced Mechano Growth Factor (MGF) when used intramuscularly. This is accomplished by surrounding part of the peptide with a structure of polyethylene glycol, which can be attached to a protein molecule. The polyethylene glycol groups protect the peptide but do not surround it completely. The active sites of the peptide are still free to do their biological function. In this case the shell is a negative charged shield against positively charged compounds that would affect the protein.
Important Notification: All of our products and services listed in this website are for research or production use only, not for direct human use.