Work with cell cultures and experiments with animals have shown that administration of thymosin β4 can promote migration of cells, formation of blood vessels, maturation of stem cells, survival of various cell types and lowering of the production of pro-inflammatory cytokines. These multiple properties have provided the impetus for a worldwide series of on-going clinical trials of potential effectiveness of thymosin β4 in promoting repair of wounds in skin, cornea and heart.[17]
Finally, patients deficient in growth hormone who get IGF-1 injections have shown increased rates of fat loss and fat oxidation. One theory for this is that, as you’ve just learned, IGF-1 can suppress circulating insulin, which would allow more burning of fatty acids from fat cells. This makes sense, since we do know that fat cells contain IGF-1 receptors, and this means that IGF-1 can interact with fat cells.
IGF-1 isoforms are produced as a preprohormone containing a signal peptide at the amino-terminus. Removal of the signal peptide leaves the prohormone (mature peptide + E-domain), which is further cleaved to yield the mature peptide (70 amino acids) and the E-domain. Cleavage of the E-domain region occurs at a pentabasic-processing motif LysXXLys68XXArg71XXArgXXArg between the D and E-domains (Duguay et al., 1995). Disruption of this cleavage site does not impact secretion per se, but appears to modulate the activities and actions of the mature IGF-1 (Pfeffer et al., 2009; Barton et al., 2010). Interestingly, the existence of the different E-domain regions gives rise to unique isoform-specific gene expression profiles compared to those associated with mature IGF-1 (Barton et al., 2010). These data suggest the E-domains regulate aspects of IGF-1 actions whether in the prohormone form or independently upon cleavage. Given the existence of this cleavage site in all the isoforms and disruption modifies behavior, it is reasonable to hypothesize that the E-domain may have independent actions in vivo. Indeed, research to date has been directed at defining those actions in relation to MGF and the use of peptide mimetics have been insightful (see below).

Representative immunoblot analysis of the expression of endogenous MGF. The hippocampi (C-control) and postischemic at 3, 24, 48, and 72 h after reperfusion were divided into vulnerable (CA1) and the resistant (CA2-3, DGabdominal, AbP) parts. Note the rapid increase and sustained expression of MGF only in the abdominal part (arrow). There were always two immunopositive bands present; the identity of the larger-size band is not clear. Antibody was obtained by immunization with synthetic C-terminal MGF peptide shown on blots as a positive control (smaller band in MGF lane) and does not cross-react with the recombinant IGF-1 peptide (IGF-1 lane). 

Porcine chondrocytes were homogenized by mechanical disruption of the frozen tissue (liquid nitrogen) using a mortar and pestle. RNA was isolated as described in the RNeasy Mini Handbook (Qiagen, Hilden, Germany, 06/2001). Cells from monolayer culture were harvested by adding 1 ml of the TRI reagent kit (Sigma-Aldrich, St. Louis, MO, USA). RNA was isolated according to the manufacturer's instructions. The purity and amount of RNA were determined by measuring the OD260∶280 ratio.

Another benefit of CJC 1295 is its ability to promote slow wave sleep. Slow wave sleep is also known as deep sleep and is the portion of sleep responsible for the highest level of muscle growth and memory retention. SWS decreases significantly in older adults and also with people who tend to exercise later in the evening. Clinical studies have shown that a once-daily administration of CJC 1295 normalizes the GHRH response and can induce significantly deeper sleep.
Excerpt: I started taking Ipamorelin and CJC 1295 without DAC yesterday. I dont see many logs and i see a lot of people wondering what kind of results you can get wiith these peptides. I have enough to go a couple of months right now and see what this stuff is really about. Im taking each 3x a day. Morning, pwo, and before bed. Im taking 100mcgs of each in the morning and before bed. After my workout, I'll take 100mcgs of cjc and 100-200mcgs of Ipa. I weigh 215 and i have no idea what my bodyfat
I just had this test and mine was 75. I’m 49 years old. I generally eat a lot of protein so I assumed mine would be high and I wanted it outside of the parameters mentioned for breast cancer and lower overall after reading Valter Longo’s studies on middle age, high IGF-1 and cancer but now I’m concerned it might be too low. I’m slightly overweight with minimal belly fat but I do lack energy often. Not sure what to think about this number? Waiting on the results of my chem panel, CBC, hormone and lipid testing.
Yes, Ipamorelin can help you lose weight. But, if you are not exercising, and aren’t eating well, it can only do so much. There is no magical supplement which will undo laziness and a horrible diet – keep this in mind. When using it for fat loss, make sure you are exercising. Doing so will naturally increase weight loss results, as you are going to burn more calories, along with the caloric deficit you are already on, for greater results. Further, your diet matters. If you are eating 5000 calories of junk per day, no supplement will help you lose weight – no matter how potent it claims to be!

In no particular order of importance, here they are: I swallow colostrum capsules every morning, I drink raw animal milk such as camel milk and goat milk in moderation, and I use the equivalent of around 30 grams of grass-fed whey protein each day in a smoothie (if you’re vegan or if whey protein doesn’t agree with your stomach, you can combine digestive enzymes with a vegan protein such as brown rice protein, pea protein or hemp protein for an effect similar to whey protein).
Intriguingly, the MGF-24aa-E peptide has attracted considerable attention, but not from the mainstream pharmaceutical industry or the medical establishment but instead from the poorly regulated or outright illegal branches of pharma: the MGF-24aa-E peptide has become an important component of the readily available anabolic and doping products and there may be a number of reasons for this peculiar situation.
One combination of natural supplements that boost IGF-1 with no injections required would simply be a one-two combo of whey protein and colostrum. Throw small bits of natural dairy into the mix and you’ve got a pretty potent trilogy for not just increasing IGF-1, but also all the fat loss, lean muscle gain, and cellular repair mechanisms that accompany a surge in growth hormone.
Several research groups have found that aberrant expression of Tβ4 is associated with metastasis and invasion of tumor cells in colorectal carcinoma, gastrointestinal stromal tumors, and breast cancer [19–21]. Here, we found that Tβ4 gene silencing led to the inhibition of migration and invasion of NSCLC cells and a significant decrease in the expression of the invasion-related protein MMP-2. The underlying molecular signaling mechanism of Tβ4 in cell invasion and migration has been reported in various types of cells. It has been shown that Tβ4 induces invasion and migration of human colorectal cancer cells through the integrin-linked kinase (ILK)/AKT/β-catenin signaling pathway [8]. Regulation of glycogen synthase kinase-3 by Tβ4 has been associated with gastric cancer cell migration [22]. Tβ4 induced colon cancer cell migration and clinical metastasis by enhancing the ILK/IQGAP1/Rac1 signal transduction pathway [23]. Therefore, the participation of these pathways or proteins in Tβ4-mediated NSCLC cell invasion and migration should be further explored.
Numerous sources have claimed that Deer Antler Spray, purportedly extracted from cervid sources, contains IGF-1.[39][40][41][42] Credence to this claim comes from the fact that deer's antlers grow extremely rapidly and that the associated cellular factors can similarly aid in skeletal healing in humans. IGF-1 is currently banned by various sporting bodies. However, sprays and pills claiming to be 'deer antler velvet extracts' are freely available on the market.[43] As IGF-1 is a protein, it is poorly absorbed orally since it is rapidly broken down in the gastrointestinal tract; and large molecular weight and high hydrophilicity prevents it from being absorbed by intestinal tissue.[44][45] In September 2013, the headquarters of SWATS, a well-known distributor of deer antler spray and other controversial products, was raided and ordered to shut down by Alabama's attorney general citing "numerous serious and willful violations of Alabama’s deceptive trade practices act".[46][47] Deer antler spray has been linked to prion disease.[48]

Seminal work examining the translation and stability of Igf1 gene products demonstrated that human fibroblasts secrete an approximately 21.5-kDa peptide (13); additionally, in vitro translation of human IGF-IEa and IGF-IEb mRNAs revealed major bands of approximately 17.5 kDa for IGF-IEa and approximately 22 kDa for IGF-IEb (14). The existence of high relative molecular mass (Mr) IGF-I molecules was also shown using in vitro translation with rat IGF-IEa and IGF-IEb mRNA sequences (15). Collectively, these data suggest that the E-peptides are indeed translated and exist as a part of pro-IGF-I. Indeed, antiserum directed against a 13-amino-acid peptide with sequence identical to a portion of the E-domain of human IGF-IEa recognized a protein of approximately 19 kDa as determined by SDS-PAGE (16), and antiserum developed against a 23-amino-acid peptide with a sequence identical to a portion of the human Eb peptide was immunoreactive with molecules of various sizes that were presumed to represent precursor forms of IGF-I (17). Although these observations suggest that the E-peptides are stable as part of pro-IGF-I, whether they are stable or functional apart from the pro-IGF-I molecule is unknown. An approximately 2-kDa band (consistent with the Mr of the Ea peptide) was recognized by an IGF-IEa monoclonal antibody in FLAG-pro-IGF-IEa-transfected HEK293 cells, suggesting that a stable Ea peptide is generated under these conditions; however, this band was not evident in nontransfected IM9 lymphocytes (18). Investigation into the stability, secretion, and functions of the various E-peptides is currently ongoing, and recent work indicates a possible role for these peptides in mediating cellular uptake of IGF-I (19).
IGF-1 is so named because of its close resemblance to insulin. Because IGF-1 is so similar to insulin, it interacts with insulin receptors on the surface of your cells, produces some of the same effects as insulin and even magnifies the effect of insulin. For example, one primary effect of both excess insulin and excess IGF-1 is hypoglycemia (low blood glucose). When you workout for a long time (longer than about one hour) your liver increases its release of IGF-binding protein (IGFBP-3) to prevent the onset of hypoglycemia that would otherwise happen as a result of the increased release of IGF-1 that occurs during training.
Osteosarcoma is one of the most common bone tumors, and exhibits a high degree of malignancy. Gene therapy is a novel approach to its treatment, however, specific target genes are required to enable effective use of this therapy. In order to investigate the effects of the mechano‑growth factor E (MGF‑E) peptide, which is derived from the IGF‑I alternative splicing isoform, on the regulation of the development of osteosarcoma, the expression of MGF was detected in osteosarcoma cell lines with different degrees of malignancy. Concomitantly, exogenous MGF‑E peptide was used to stimulate these osteosarcoma cell lines. The results demonstrated that MGF was overexpressed in malignant osteosarcoma cells, while it was not expressed in the least malignant osteosarcoma cells. Furthermore, MGF‑E treatment altered the cell cycle distribution, and promoted the proliferation, migration and invasion of osteosarcoma cells. The possible mechanisms underlying these effects were detected by quantitative polymerase chain reaction and western blotting. Based on these results, it was hypothesized that MGF may be a suitable biomarker for malignant osteosarcoma phenotypes.

These proteins became of interest in neurobiology with the finding that in the nudibranch (sea slug) Hermissenda crassicornis, the protein Csp24 (conditioned stimulus pathway phosphoprotein-24), with 4 repeats, is involved in simple forms of learning: both one-trial enhancement of the excitability of sensory neurons in the conditioned stimulus pathway,[25] and in multi-trial Pavlovian conditioning.[26] The phosphorylation of Csp24, in common with post-translational modifications of a number of cytoskeleton-related proteins may contribute to actin-filament dynamics underlying structural remodeling of responsive cells.[26]
It is also important to note that whether you are a long-time user or a first-time user of Ipamorelin, your body is going to react differently to that of the next user. Like the benefits you will experience, the side effects you are going to experience will occur differently, and at different dosage levels. So, it truly is a trial and error period you are going to go through with a test run of Ipamorelin for new users. You have to find what works for you, how your body will react, and what potential side effects are lingering ahead, in order for you to achieve the greatest results, and eventually find the proper dosage and cycle level, which is going to work the best for your body and system.
In the heart, there is temporal regulation of both MGF and IGF-IEa mRNA expression in response to ischemia associated myocardial infarction. MGF expression is induced within one hour and remains elevated for up to 8 weeks whereas the IGF-Ea appears after 4 days (Stavropoulou et al., 2009). These expression profiles suggest that the isoforms play distinct and separable roles in local adaptation aimed at mitigating tissue damage to augment cardiac output. Moreover, intracoronary delivery of the MGF-24aa-E peptide elicits myocardial protection and improves hemodynamic function to a greater extent than mature IGF-1 following myocardial infarction in sheep. As the analog does not have the IGF-1 receptor (IGF-1R) binding site, the mechanisms of action may differ (see below). Limited mechanistic findings suggested that the cellular protection conferred by the MGF-24aa-E peptide, was due to an inhibition of apoptosis in the infarct border zone (Carpenter et al., 2008). However, given the growing data showing effects of the MGF-24aa-E peptide on various precursor cell populations, it is an intriguing notion to speculate that similar effects may exist on cardiac precursor cell populations to aid in repair and recovery of the heart. It is well known the heart has a limited capacity for regeneration, but recent studies have shown the existence of resident populations of multipotent precursor cells (Segers and Lee, 2008). These cells exist in extremely low numbers but if stimulated, could provide an endogenous source for the different lineages (cardiac, endothelia, and vascular) needed to initiate regeneration. To this end, the MGF-24aa-E peptide has been shown to increase proliferation and migration of mesenchymal bone marrow derived stem cells, which have been proposed as a source of autologous stem cells for transplantation into the heart (Collins et al., 2010). In addition, the MGF-24aaE peptide appears to stimulate pro-angiogenic activities in human vascular endothelial cells (Deng et al., 2012). Thus, delivery of the MGF-24aa-E peptide could bestow potentially useful therapeutic actions at the level of vascular regeneration and collateralization, to restore blood flow in the heart following myocardial infarction.
The group had first identified the thymosin sulfoxide as an active factor in culture fluid of cells responding to treatment with a steroid hormone, suggesting that its formation might form part of the mechanism by which steroids exert anti-inflammatory effects. Extracellular thymosin β4 would be readily oxidised to the sulfoxide in vivo at sites of inflammation, by the respiratory burst.[21]