HGH 36 IU – Genotropin 36 Cartridge by Pfizer
ONE ORDER UNIT INCLUDES: 1 cartridge contains 36 IU
1 VIAL CONTAINS:36 IU
TOTAL CARTRIDGES PER ONE ORDER UNIT: 1
TOTAL IU PER ONE ORDER UNIT: 36 IU
ALTERNATIVE STEROID NAMES: Genotropin, HGH, Human growth hormone, Saizen, Somatohorm, Nutropin, Genotropin Pfizer, Humatrope, HGH Somatripin, Somatropin
ACTIVE SUBSTANCE: Human growth hormone
DESCRIPTION: Genotropin, also commonly referred to as human growth hormone (HGH), is a hormone that is produced in the human body and excreted into the blood by the somatotrope cells of the anterior pituitary gland. It is a single-chain protein that is composed of 191 amino acids with a molecular weight of approximately 22,000 Daltons.
GH secretion has many direct and indirect effects on the human body. First, GH stimulates the liver’s production of insulin-like growth factor (IGH-1). Because GH stimulates the liver’s production of IGF-1, the effects of both GH and IGF-1 are listed below.
Synthetic version of Human Growth Hormone is called Somatropin (191 amino acid sequence growth hormone). Somatropin is identical to human body’s own GH.
Genotropin (Somatotropin; generic name Human Growth Hormone) by Pfizer is used for: Growth Hormone Deficiency, Treatment for small gestational age (SGA) and intrauterine growth retardation (IUGR), Idiopathic Short Stature, AIDS Wasting and Cachexia, Short Stature Caused by Turner’s Syndrome, Short Stature Caused by Prader-Willi Syndrome, Growth Problems Caused by Short Bowel Syndrome, Improper Growth in Children with Renal Disease, Body Building Enhancement Drug, Weight Loss Drug, Anti-Aging Drug, Treatment for Children with Rheumatoid Arthritis, Osteoporosis Treatment, Teatment for Children with X-Linked Hypophosphatemic Rickets (XLH)
IGF1 LR3 allows for many of the growth-promoting effects of growth hormone insulin-like growth factors also know as IGF’s. IGF-1 LR3 comprises a family of peptides (protiens) that play important roles in mammalian growth and development. IGF1 LR3 is also known as Long R3 IGF-1 or Insulin-Like Growth Factor-I Long Arg3.
The Long R3 IGF-1 version is significantly more potent than regular IGF-1. The enhanced potency is due to the decreased binding of IGF1 LR3 to all known IGF binding proteins. These binding proteins normally inhibit the biological actions of IGF’s therefore IG-1 LR3 has been shown to have increased efficacy and function .
This IGF-1 LR3 analog of IGF-1 has been created with the purpose of increasing the biological activity of the IGF peptide.
IGF1 LR3 is also known as Long R3 IGF-1 or Insulin-Like Growth Factor-I Long Arg3. This is a human recombinant, single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9200 Daltons. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’.
IGF-1 LR3 is the primary protein involved in responses of cells to growth hormone (GH): that is, IGF-I is produced in response to GH and then induces cellular activities. One such example is muscle growth or hyperplasia. This compound also makes the human body more sensitive to insulin. It is the most potent growth factor found in the human body. IGF-1 causes muscle cell hyperplasia, which is an actual splitting and forming of new muscle cells.
The most effective form of IGF-1 is considered to be IGF-1 LR3. This formula has been chemically altered to avoid binding to proteins in the human body, and to increase the half life, approximately 20-30 hours
Follistatin 344 (FST-344)
Follistatin (FST) is a secreted glycoprotein that was first identified as a folliclestimulating hormone inhibiting substance in ovarian follicular fluid (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa) protein with a 29 aa signal sequence, an Nterminal atypical TGF binding domain, three Follistatin domains that contain EGFlike and kazallike motifs, and a highly acidic Cterminal tail. Follistatin is a secreted protein that binds to ligands of the TGF-Beta family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-Beta ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-Beta1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 37.8 kDa protein containing 344 amino acids.
ACVR2B or Activin Receptor Type II B, is also known as ActR-IIB and MGC116908, ACVR2B is an activin type 2 receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Buy ACVR2B, myostatin blocker (research peptide/protein) of high quality only at Superior Peptide.
Myostatin (GDF8) is a negative regulator of muscle growth in mammals, and loss-of-function mutations are associated with increased skeletal-muscle mass in mice, cattle, and humans. Here, we show that positive natural selection has acted on human nucleotide variation at GDF8, since the observed ratio of nonsynonymous:synonymous changes among humans is significantly greater than expected under the neutral model and is strikingly different from patterns observed across mammalian orders. Furthermore, extended haplotypes around GDF8 suggest that two amino acid variants have been subject to recent positive selection. Both mutations are rare among non-Africans yet are at frequencies of up to 31% in sub-Saharan Africans. These signatures of selection at the molecular level suggest that human variation at GDF8 is associated with functional differences.
The genetic basis of muscle development and growth has been extensively studied in an effort to treat myopathies1 and to understand individual variation in athletic performance.2 Because musculature features might have provided a fitness advantage during human evolution, candidate genes related to musculature may have been targets of natural selection in humans.
The myostatin gene, also called “growth and differentiation factor 8” (GDF8 [MIM 601788]) encodes a negative regulator of skeletal-muscle growth.3 First described in the mouse, myostatin is expressed in different muscles throughout the body, both during early development and in adults. Mouse null mutants are significantly larger than wild-type animals, with 200%–300% more skeletal-muscle mass because of an increase in the number of myocytes (hyperplasy) and an increase in the size of muscle fibers (hypertrophy).3 A similar phenotype is seen in some breeds of double-muscled cattle that also have myostatin mutations.4,5 A loss-of-function mutation in the myostatin gene (a missplicing change in IVS1:G378A) has been associated with muscle hypertrophy in a human subject,6 and myostatin expression levels have been shown to be inversely correlated with muscle mass in healthy and HIV-infected subjects.7 These data suggest that myostatin acts in a similar fashion among all mammals. Here, we tested the hypothesis that patterns of human nucleotide variation at GDF8 have been shaped by positive natural selection.
TB-500 (Thymosin Beta-4)TB-500 is a synthetic version of the naturally occurring peptide present in virtually all human and animal cells, Thymosin Beta-4. This potent peptide is a member of a ubiquitous family of 16 related molecules with a high conservation of sequence and localization in most tissues and circulating cells in the body. TB-500 not only binds to actin, but also blocks actin polymerization and is the actin-sequestering molecule in eukaryotic cells.
TB-500 was identified as a gene that was up-regulated four-to-six fold during early blood vessel formation and found to promote the growth of new blood cells from the existing vessels. This peptide is present in wound fluid and when administered subcutaneously, it promotes wound healing, muscle building and speeds up recovery time of muscles fibres and their cells. An additional key factor of TB-500 is that it promotes cell migration through a specific interaction with actin in the cell cytoskeleton. It has been demonstrated that a central small amino acid long-actin binding domain has both blood cell reproduction and wound healing characteristics. These characteristics are uncovered by accelerating the migration of endothelial cells and keratinocytes. It also increases the production of extracellular matrix-degrading enzymes.
Studies demonstrate that TB-500 is a potent, naturally occurring wound repair factor with anti-inflammatory properties. Tß4 is different from other repair factors, such as growth factors, in that it promotes endothelial and keratinocyte migration. It also does not bind to the extracellular matrix and has a very low molecular weight meaning it can travel relatively long distances through tissues. One of TB-500 key mechanisms of action is its ability to regulate the cell-building protein, Actin, a vital component of cell structure and movement. Of the thousands of proteins present in cells, actin represents up to 10% of the total proteins which therefore plays a major role in the genetic makeup of the cell.
Effects of TB-500 Demonstrated In Recent StudiesRecent laboratory research and clinical studies conducted using TB-500 (Thymosin Beta 4) have shown that it may promote the following:
• Endothelial (blood vessels) cell differentiation• Angiogenesis (growth of new blood cells from pre-existing vessels) in dermal tissues• Keratinocyte migration• Collagen deposition• Decreases inflammation of tissue in joints• Increase muscle growth with huge increases in endurance and strength noted• Relaxed muscle spasm and improved muscle tone• Increase the exchange of substance between cells• Encourage tissue repair• Stretches connective tissue and helps maintain flexibility• Prevents the formations of adhesions and fibrous bands in muscles, tendons and ligaments.
Secretary growth hormone with exclusively owned patent of protein stabilizer Growth hormone (GH) is a kind of peptide hormone secreted by anterior pituitary (adenohypophysis), the weight of human pituitary is about 0.5 g and the content of GH is extremely low. In 1955, human growth hormone (hGH) was separated from human pituitary, and in 1979, the hGH gene was cloned. hGH is a single-stranded peptide containing 191 amino acid and disulfide bonds with the molecular weight of 22,000. The main physiological action of GH is to promote growth and development, and its receptors is distributed in various tissues all over the body. The physiological function of growth hormone is mainly to promote the growth of cartilages, bones and cells to perform tissue repair and regulate metabolism.HGH is composed of 191 amino acid, which is completely identical with natural human growth hormone and has the same efficacy without adverse reaction. The SDS-PAGE electrophoresis test almost presents no dimmer due to the exclusively owned protein stabilizer of growth hormone. The volume exclusion high efficiency liquid chromatography (HPLC) analysis indicated that its purity is 99.9% and the content of polymer protein is only 0.1%, which lies in the most advanced level in the world.Quality Inspection
The volume exclusion high efficiency liquid chromatography analysis indicated that the purity of the batched final products of HGH is 99.9% which greatly surpasses the purities of domestic known related products. Growth hormone protein stabilizer techniqueLeading technical advantages of HGH Secretary expression technique
The target protein with extracellular signal peptide folds into natural configuration, which ensures the complete identity of the structures of HGH and natural growth hormone and the activity of the product is 100%. The fragility of outer cell wall increases, therefore, the inner cell wall keep integrate and contamination of bacterial protein to the growth hormone is extremely low so that the purity is very high. Growth hormone protein stabilizer technique
The decay of biological activity of HGH within the expiry date is extremely low so it is very stable. This feature ultimately ensures the therapeutic effect of the drug and avoids the adverse reactions including red swelling, pain , etc during the administration.
PT-141, commonly known as PT141 or Bremelanotide, is a synthetic heptapeptide analogue of the naturally occuring alpha-Melanocyte stimulating hormone (α-MSH) that is currently being studied for its numerous theoretical therapeutic applications. Alpha-MSH has potent influence over lipid metabolism, appetite, and sexual libido. PT-141 Bremelanotide, a metabolite of its predecessor Melanotan II, has the amino acid sequence Ac-Nle-cyclo[Asp-His-D-Phe-Arg-Trp-Lys]-OH and a molecular weight of 1025.2 Dalton. In initial testing, Melanotan II did induce melanogenesis, but additionally caused sexual arousal and spontaneous erections as unexpected side effects in nine out of the ten original male volunteer test subjects. Alpha-MSH activates certain melanocortin receptors in the process of exerting its effects. Resultantly, PT-141 has been shown in studies to exhibit libido-enhancing effects by activating melanocortin receptors. PT 141 has been researched extensively for its possible treatment of male sexual dysfunction (erectile dysfunction or impotence), female sexual dysfunction (sexual arousal disorder), hemorrhagic shock and reperfusion injury.
PMGF (Mechano Growth Factor) IGF-1 EcMechano growth factor (MGF) is a novel splice variant of the Insulin-Like Growth Factor-1 (IGF-1), also known as IGF-1 Ec in humans and IGF-1Eb in rodents. It is actually originally called MGF because the RNA form of it is expressed in muscle tissues in response to the overload or/and damage of muscle growth tissue. The C-terminal peptide of the mechano growth factor (MGF) is a crucial region for the alternative splicing of the peptide. The alternative splicing in the MGF is brought about by the shift in the reading frame in which a specific C-terminal sequence (E-domain) is encoded by exon 5 and the first part of the exon 6. Another interesting point in MGF is that, because of the E domain it contains, MGF can act on muscles independently from the rest of the molecule. Furthermore, MGF can elicit very different effects with mGF promoting satellite cells proliferation and IGF-1 inducing differentiation (Dluzniewska et al. 2005).
Age Related Muscle Loss and MGFMGF was suggested to play a number of physiological roles because the failure in its expression may result to age-related loss of skeletal function. Included in its functions is its ability to become a potent neuroprotective as supported by the study that has shown functional copies of the MGF cDNA to be expressed in a plasmid vector which then protected facial neurons after nerve damage (Dluzniewska et al. 2005). One such failure is called sarcopenia. It would also appear that with regards to age, the young have a better ability to respond to MGF (4), and that the elderly experience a decreased response to MGF which results in a decreased ability to stimulate the growth of new muscle tissue.
How does Mechano Growth Factor work? – Muscle Growth!When mechanical overload is introduced to a muscle (as by weight training), the IGF-1 gene is released and is differentially spliced during the bodies response. Initially, it it is spliced to produce predominantly IGF-1Ec (called the MGF splice variant of IGF-1). This early splicing stimulates satellite cells into activation. Which in turn allows the activation of extra undamaged nuclei to grow new muscle fiber and tissue. The appearance of MGF also initiates the upregulation of new protein synthesis. After this initial splicing of IGF-1 into MGF, production then switches towards producing a systemic release of IGF-1Ea from the liver, which also upregulates protein synthesis as well. The expression of IGF-1 splice variants, over the course of the healing and regrowth phase of muscle repair is thought to be the primary mechanism by which the body produces new muscle tissue.
Recent Research and Studies Involving Mechano Growth FactorInsulin like growth factor-1 (IGF-1) expression is implicated in myocardial pathophysiology, and two IGF-1 mRNA splice variants have been detected in rodents, IGF-1Ea and mechano-growth factor (MGF). Recent research has shown that the expression pattern of IGF-1 gene transcripts in rat myocardium from 1 h up to 8 wks after myocardial infarction induced by left anterior descending coronary artery ligation. In addition, we characterized IGF-1 and MGF E peptide action and their respective signaling in H9C2 myocardial-like cells in vitro. IGF-1Ea and MGF expression were significantly increased, both at transcriptional and translational levels, during the late postinfarction period (4 and 8 wks) in infarcted rat myocardium. Measurements of serum IGF-1 levels in infarcted rats were initially decreased (24 h up to 1 wk) but remained unaltered throughout the late experimental phase (4 to 8 wks) compared with sham-operated rats. Furthermore, specific antiâ€“IGF-1R neutralizing antibody failed to block the synthetic MGF E peptide action, whereas it completely blocked IGF-1 action on the proliferation of H9C2 cells. Moreover, this synthetic MGF E peptide did not activate Akt phosphorylation, whereas it activated ERK1/2 in H9C2 rat myocardial cells. These data support the role of IGF-1 expression in the myocardial repair process and suggest that synthetic MGF E peptide actions may be mediated via an IGF-1R independent pathway in rat myocardial cells, as suggested by in vitro experiments.
Recent studies have also discovered two clones of the hybridonoma secreting monoclonal antibodies to the mechano-growth factor have been developed by cell fusion technique. The monoclonal antibody of one clone recognizes the human MGF peptide that is absent in insulin-like growth factor-1 (IGF-1) which comprised mostly of amino acids from 87-111. Enzyme-linked immunosorbent assay (ELISA) has further shown that there is a high affinity binding constants with the full length of the MGF and the 87-111 fragments of the clones. These can then be used for the quantitation of the MGF through sandwich type assay (Kravchenko et al. 2006).
PEG MGF (Pegylated Mechano Growth Factor)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, namely Mechano 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 MGFMechano 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.