Moppy1
New member
I know we have covered all this before in other threads, but the community does not seem to understand. First, IGF-1 and HGH are completely different gene products, and they are not related whatsoever, nor does one come from the other. The only relatedness is the fact that HGH binding to the HGH receptor stimulates production and secretion of IGF-1 from the liver, which is actually how HGH stimulates growth during development, and also muscle growth later in life (it is all mediated by IGF-1 secretion).
Second, recombinant protein production means that an organism, typically a bacterium (such as e. coli) is programmed to generate the protein in large fermentors, which is then collected in some manner under conditions that allow IGF1 to fold properly, or maintain its folded conformation, followed by a robust purification process. IGF-1 has 3 internal disulfide bonds that have to be generated in a living organism for the protein to have the properly folded confirmation. Chemical synthesizers can also be used to make IGF-1. Chemical synthesizers simply add consecutive amino acids together in their prescribed order, which generates the full length protein, but this will definitely not lead to the proper folding of the protein, or to the formation of the critical disulfide bonds. Although this definitely generates IGF1 protein and at about 1/50th of the cost. But, synthesized IGF-1 as it comes off the peptide synthesizers is useless.
Third, real IGF-1 is definitely more expensive than HGH on a milligram basis, although IGF-1 is more potent than HGH so less can be used, but even given this IGF-1 if properly sourced and active, is many fold more expensive. And real IGF1 that is biologically active is much much harder to reliably acquire because it is harder to make and the protocols and preprogrammed bacteria are not standardized like it is for HGH. Very few companies make it correctly, and even when they do, it varies from lot to lot. Not wanting to disclose to much, but I know all these things first hand given my profession. The cell culture based assays do work for testing IGF1 activity, but the best way to test a lot is to inject mice for 6 weeks and see how much they grow. You would be surprised at how much lots vary even from the same vendor that is a known reliable source (all recombinant of course).
RUI's IGF1 could indeed be good to go. Never tried it. But definitely use BAC water and not acetic acid if you have to resuspend it. Clinical grade IGF1 that is used in human trails comes in liquid form on ice, as this is the best way to insure activity is maintained (not from lyophilized powder or frozen).
Second, recombinant protein production means that an organism, typically a bacterium (such as e. coli) is programmed to generate the protein in large fermentors, which is then collected in some manner under conditions that allow IGF1 to fold properly, or maintain its folded conformation, followed by a robust purification process. IGF-1 has 3 internal disulfide bonds that have to be generated in a living organism for the protein to have the properly folded confirmation. Chemical synthesizers can also be used to make IGF-1. Chemical synthesizers simply add consecutive amino acids together in their prescribed order, which generates the full length protein, but this will definitely not lead to the proper folding of the protein, or to the formation of the critical disulfide bonds. Although this definitely generates IGF1 protein and at about 1/50th of the cost. But, synthesized IGF-1 as it comes off the peptide synthesizers is useless.
Third, real IGF-1 is definitely more expensive than HGH on a milligram basis, although IGF-1 is more potent than HGH so less can be used, but even given this IGF-1 if properly sourced and active, is many fold more expensive. And real IGF1 that is biologically active is much much harder to reliably acquire because it is harder to make and the protocols and preprogrammed bacteria are not standardized like it is for HGH. Very few companies make it correctly, and even when they do, it varies from lot to lot. Not wanting to disclose to much, but I know all these things first hand given my profession. The cell culture based assays do work for testing IGF1 activity, but the best way to test a lot is to inject mice for 6 weeks and see how much they grow. You would be surprised at how much lots vary even from the same vendor that is a known reliable source (all recombinant of course).
RUI's IGF1 could indeed be good to go. Never tried it. But definitely use BAC water and not acetic acid if you have to resuspend it. Clinical grade IGF1 that is used in human trails comes in liquid form on ice, as this is the best way to insure activity is maintained (not from lyophilized powder or frozen).
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