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Amino Acid Peptides IGF-1 LR3 for Increased Biological Activity CAS 946870-92-4
WHAT IS IGF-1 LR3?
IGF-1 LR3, also known as Long Arg3 IGF-1, is a recombinant protein analogue of human Insulin-Like Growth Factor-1 that has a molar mass of 9,200 Daltons and is comprised of 83 amino acids. IGF-1 LR3 comprises the complete IGF-1 sequence, but with a 13 amino acid extension on the B-Terminus domain and the substitution of an Arginine for the Glutamic Acid at position 3. The LR3 analogue of IGF-1 was created with the intent to drastically increase the biological activity of the protein and IGF-LR3 is several times more potent than rhIGF-1. This specific sequence alteration has decreased the affinity of binding to the IGFBPs, which control the biological actions of IGF-1 and prevent the protein from reaching the IGF-1 receptors.
IGF-1 LR3 is an 83 amino acid analogue of human IGF-1 that has been modified to include a 13 amino acid extension on its N-Terminus and the substitution of an Arginine amino acid for Glutamine at position 3. While IGF-1 LR3 is comprised of the the complete human IGF-1 sequence, these modifications have rendered the LR3 version to be much more potent than IGF-1 in-vitro and in-vivo. The result of these modifications is that IGF-1 LR3 does not bind as strongly to the IGFBPs, which modify the biological actions of IGF-1. Resultantly, IGF-1 LR3 binds to the type 1 IGF-1 receptor with similar affinity to that of wild type IGF-1, but with higher biological activity and has several advantages over recombinant insulin. The supplementation of mammalian cell cultures with Long R3 IGF-1 at a much lower concentration results in more highly elevated productivity than with standard concentrations of insulin and/or standard IGF-1. IGF-1 LR3 is better able to stimulate the type 1 IGF receptor and thus induce a higher level of activation of intracellular signaling, which is responsible for promoting cell proliferation and the inhibition of apoptosis.
What is the Amino Acid Sequence of IGF-1 LR3?
The amino acid sequence (three letter) is Met-Phe-Pro-Ala-Met-Pro-Leu-Ser-Ser-Leu-Phe-Val-Asn-Gly-Pro-Arg-Thr-Leu-Cys-Gly-Ala-Glu-Leu-Val-Asp-Ala-Leu-Gln-Phe-Val-Cys-Gly-Asp-Arg-Gly-Phe-Tyr-Phe-Asn-Lys-Pro-Thr-Gly-Tyr-Gly-Ser-Ser-Ser-Arg-Arg-Ala-Pro-Gln-Thr-Gly-Ile-Val-Asp-Glu-Cys-Cys-Phe-Arg-Ser-Cys-Asp-Leu-Arg-Arg-Leu-Glu-Met-Tyr-Cys-Ala-Pro-Leu-Lys-Pro-Ala-Lys-Ser-Ala
Receptor Grade vs Media Grade IGF-1 LR3
Genuine Receptor Grade LR3 IGF-I is a high quality research reagent for use in studies on cell growth, IGF receptors and IGF binding proteins and is more potent than rH IGF-1 and Media Grade IGF-1 LR3 both in vivo and in vitro due to the drastic increase in biological activity (stronger affinity for binding with the IGF receptor) and high-level purity. This combination of increased biological activity and purity is what sets Receptor Grade IGF-1 LR3 apart from standard IGF-1. Media grade LR3 IGF-I is more commonly used in commercial cell culture vs mammalian. It can also be used as a research reagent at an economical cost to enable studies where biological potency is of less value and higher quantities are required. To maximize results in an animal-based cell study or production Receptor Grade IGF-1 Long R3 should be used exclusively.
IGFB Binding and Increased Biological Activity
By resisting IGFBP-binding, IGF-1 LR3 has a greater physiologic effect than IGF-1 does. The longer duration of action allows for smaller amounts to be used with the same effects. Some IGF-1 derivatives, such as the GPE derivative, made up of just the last three N-terminal amino acids of the IGF-1 protein, have been shown to have therapeutic effects in neurological injuries like stroke. Most studies concerning the effects of IGF-1 derivatives have been carried out in animal models, with little to no data available for humans.
Insulin Like Growth Factor Receptor Interactions
IGF-1 Long R3 binds to at least two cell surface receptors: IGF-1R and the insulin receptor. The IGF-1 receptor is referred to as the "physiologic" receptor because IGF-1 binds to it with significantly higher affinity (approximately 100 times higher) than it does to the insulin receptor. By binding to IGF-1R, IGF-1 can affect metabolism, cell growth (hypertrophy), differentiation and cell division (hyperplasia), prevention of cell death (apoptosis), normal development, and even malignant growth. IGF-1R has been implicated in several different types of cancer include breast, prostate, and lung cancer. IGF-1 also binds to the insulin receptor and activates it, thereby encouraging cells to take up glucose from the blood stream. The effects of IGF-1 on muscle cells are three-fold. Firstly, IGF-1 encourages hyperplasia, or an increase in the number of muscle cells. Secondly, IGF-1 has a strong effect on skeletal muscle - In regards to the life span of satellite cells. Satellite cells support muscle cells, providing them with needed nutrients and helping them to operate efficiently.
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